Study Guide Basic Biochemistry Semester I 28 Desember 2015
Study Guide Basic
Biochemistry
PLANNERS TEAM
No.
NAME
PHONE
1.
Dr.dr. Desak Made Wihandani, M.Kes
Head
081338776244
2.
Dr.ret.nat.dr. Ni Nyoman Ayu Dewi
Secretary
081337141506
3.
Prof.dr. I Nyoman Agus Bagiada,
SpBiok
Member
081338338611
4.
dr. I Wayan Surudarma, M.Si
Member
081338486589
5.
dr. I Wayan Gede Sutadarma, M.Gizi,
SpGK
Member
087862155380
6.
dr. Ida Ayu
M.Biomed
7
Dr. Ni Wayan Tianing, SSi, M.Kes
Dewi
Wiryanthini, Member
Udayana University Faculty of Medicine, DME, 2015
Member
08123625239
08123982504
1
Study Guide Basic
Biochemistry
~FACILITATORS ~
NO
GROUP
DEPT
PHONE
VENUE
1
Radiology
081805673099
2
Dr.dr. Elysanti Dwi Martadiani,
Sp.Rad
dr. Reni Widyastuti, S.Ked
2
Pharmacology
08174742501
3
dr. Ni Ketut Putri Ariani, Sp.KJ
3
Psychiatry
082237817384
4
dr I Gusti Agung Gede Utara
Hartawan, Sp.An, MARS
dr. Ni Luh Ariwati
4
Anasthesi
08123868126
5
Parasitology
08123662311
6
Histology
08124665966
7
Microbiology
08553711398
8
dr. I G Kamasan Nyoman
Arijana, M.Si, Med
Dr.dr. Ni Nyoman Sri
Budayanti, Sp.MK(K)
dr. Ni Nyoman Mahartini, Sp.PK
8
081337165577
9
dr. I Wayan Sugiritama, M.Kes
9
Clinical
Pathology
Histology
10
dr. Ryan Saktika Mulyana,
M.Biomed, Sp.OG
10
Obgyn
082147087905
2nd floor:
R.2.01
2nd floor:
R.2.02
2nd floor:
R.2.03
2nd floor:
R.2.04
2nd floor:
R.2.05
2nd floor:
R.2.06
2nd floor:
R.2.07
2nd floor:
R.2.08
2nd floor:
R.2.21
2nd floor:
R.2.22
GROUP
1
DEPT
Forensic
PHONE
081338472005
2
Pediatri
081353027973
3
dr. I Nyoman Budi Hartawan,
M.Sc., Sp.A(K)
dr. I Wayan Surudarma, M.Si
3
Biochemistry
081338486589
4
dr. I Gusti Ayu Artini, M.Sc
4
Pharmacology
08123650481
5
dr. I Ketut Mariadi, Sp.PD
5
Interna
08123853700
6
Dr.dr. Ni Made Linawati, M.Si
6
Histology
081337222567
7
dr. I Nyoman Gede Wardana, M
Biomed
dr. I Wyn Subawa, Sp.OT
7
Anatomy
087860405625
8
Orthopaedy
Dr.rer.Nat. dr. Ni Nyoman Ayu
Dewi, M.Kes
dr. I Komang Arimbawa, Sp.S
9
Biochemistry
081338913087
081337096388
081337141506
10
Neurology
081338226892
1
5
6
7
NAME
08164732743
ENGLISH CLASS
NO
1
2
8
9
10
NAME
dr. Kunthi Yulianti, Sp.KF
Udayana University Faculty of Medicine, DME, 2015
VENUE
2nd floor:
R.2.01
2nd floor:
R.2.02
2nd floor:
R.2.03
2nd floor:
R.2.04
2nd floor:
R.2.05
2nd floor:
R.2.06
2nd floor:
R.2.07
2nd floor:
R.2.08
2nd floor:
R.2.21
2nd floor:
R.2.22
2
Study Guide Basic
Biochemistry
TIME TABLE BLOCK BASIC BIOCHEMISTRY (Dec, 28, 2015 - Jan, 15, 2016)
Day
Date
1
Monday,
Dec,
28,
2015
2
Tue, Dec,
29, 2015
Topic
Introduction
Biochemistry
Elementer
Carbohydrate
Learning
situation
to
Elementer Lipid
Elementer Protein
Protein metabolism
3
4
Wed, Dec,
30, 2015
Thursday,
Dec,31,
2015
Carbohydrate
Metabolism 1
Carbohydrate
Metabolism 2
Lipid metabolism 1
Lipid Metabolism 2
5
Mon, Jan,
4, 2016
6
Tue, Jan, 5,
2016
7
8
Wed, Jan,
6, 2016
Thu, Jan, 7,
2016
Intermetabolism
relationship
Enzyme
Bioenergetics
Phosphorylation
Oxydation
Vitamin and Mineral
Free Radical & Anti
oxidant
Matrix extracelular
Panel Discussion
9
Mon, Jan,
11, 2016
SGD & Practicum 1
10
Tue,
Jan,
12, 2016
SGD & Practicum 2
11
Wed, Jan,
13, 2016
SGD & Practicum 3
English
Class
Regular
Class
Lecture Intro
IL & L Task
Lecture 1
IL & L Task
Break
Lecture 2
Lecture 7
IL & L task
Break
Lecture 8
IL & L task
Lecture 3
IL & L task
Break
Lecture 4
IL & L task
Lecture 5
IL & L task
Break
Lecture 6
IL & L task
Lecture 9
IL & L task
Break
Lecture 10
IL & L task
Lecture 13
IL & L task
Break
Lecture 14
IL & L task
Lecture 11
IL & L task
Break
Lecture 12
IL & L task
Lecture 15
IL & L task
Plenary
08.00-09.00
09.00-10.30
10.30-11.30
11.30-13.00
13.00-14.00
14.00-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-10.00
10.00-12.00
09.00-10.00
10.00-11.30
11.30-12.30
13.30-15.00
12.30-13.30
15.00-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-11.00
12.00-14.00
SGD 1
Break
Practicum
Glucose
SGD 2
Break
Practicum Protein
SGD 3
Break
Practicum
Enzyme
08.00-10.00
10.00-11.00
11.00-15.00
13.00-15.00
12.00-13.00
08-00-12.00
08.00-10.00
10.00-11.00
11.00-15.00
08.00-10.00
10.00-11.00
11.00-15.00
13.00-15.00
12.00-13.00
08-00-12.00
13.00-15.00
12.00-13.00
08-00-12.00
Udayana University Faculty of Medicine, DME, 2015
PIC
Bagiada
Sutadarma
Sutadarma
Ayu Dewi
Ayu Dewi
Dewi
Wiryanthini
Dewi
Wiryanthini
Bagiada
Bagiada
Bagiada
Tianing
Surudarma
Surudarma
Sutadarma
Desak
Dewi
Wiryanthini
Team
Team &
Fasilitator
Team &
Fasilitator
Team &
Fasilitator
3
Study Guide Basic
Biochemistry
12
13
Thu,
Jan,
14, 2016
Friday,
Jan,15,
2016
Silent Day
Evaluation
Team
CARBOHYDRATE ELEMENTER
Abstract
Carbohydrates are major constituents of animal food and animal tissues. They are
characterized by the type and number of monosaccharide residues in their molecules.
Glucose is the most important carbohydrate in mammalian biochemistry because nearly all
carbohydrate in food is converted to glucose for metabolism. Sugars have large numbers of
stereoisomers because they contain several asymmetric carbon atoms. The
monosaccharides include glucose, the “blood sugar”; and ribose, an important constituent of
nucleotides and nucleic acids.
The disaccharides include maltose (glucosyl glucose), an intermediate in the
digestion of starch; sucrose (glucosyl fructose), important as a dietary constituent containing
fructose; and lactose (galactosyl glucose), in milk. Starch and glycogen are storage
polymers of glucose in plants and animals, respectively. Starch is the major source of
energy in the diet.
Complex carbohydrates contain other sugar derivatives such as amino sugars,
uronic acids, and sialic acids. They include proteoglycans and glycosaminoglycans,
associated with structural elements of the tis-sues; and glycoproteins, proteins containing
attached oligosaccharide chains. They are found in many situations including the cell
membrane.
Learning Task
1. Describes the characteristic of glucose, fructose and galactose
2. Describes the classification of carbohydrate
3. Identify the food sources of each carbohydrate
4. Describes the isomerism of glucose
5. Describes the characteristic of hexose and pentose sugar
6. Why the cell usually use glucose as a fuel
7. Describe the characteristic of glycogen and starch
8. Describes the characteristic of carbohydrate as a fiber
LIPID ELEMENTER
Abstract
Lipids have the common property of being relatively insoluble in water (hydrophobic)
but soluble in non-polar solvents. Amphipathic lipids also contain one or more polar groups,
making them suitable as constituents of membranes at lipid : water interfaces. The lipids of
major physiologic significance are fatty acids and their esters, together with cholesterol and
other steroids.
Long-chain fatty acids may be saturated, monounsaturated, or polyunsaturated,
according to the number of double bonds present. Their fluidity decreases with chain length
and increases according to degree of unsaturation. Eicosanoids are formed from 20-carbon
polyunsaturated fatty acids and make up an important group of physiologically and
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Study Guide Basic
Biochemistry
pharmacologically active compounds known as prostaglandins, thromboxanes, leukotrienes,
and lipoxins.
The esters of glycerol are quantitatively the most significant lipids, represented by
triacylglycerol (“fat”), a major constituent of lipoproteins and the storage form of lipid in
adipose tissue. Phosphoacylglycerols are amphipathic lipids and have important roles—as
major constituents of membranes and the outer layer of lipoproteins, as surfactant in the
lung, as precursors of second messengers, and as constituents of nervous tissue.
Glycolipids are also important constituents of nervous tissue such as brain and the outer
leaflet of the cell membrane, where they contribute to the carbo-hydrates on the cell
surface.
Cholesterol, an amphipathic lipid, is an important component of membranes. It is the
parent molecule from which all other steroids in the body, including major hormones such as
the adrenocortical and sex hormones, D vitamins, and bile acids, are synthesized.
Peroxidation of lipids containing polyunsaturated fatty acids leads to generation of free
radicals that may damage tissues and cause disease.
Learning Task
1. Describes the characteristic of lipid
2. Describes the classification of lipid
3. Identify the nomenclature methods of lipid
4. Describes the different between saturated fatty acids and unsaturated fatty acids
5. Identify the food sources of each fatty acids
6. Describes the characteristic of essential fatty acids
7. Describes the different between cis- and trans- fatty acids
8. Describes the characteristic of cholesterol
9. Describe the characteristic of lipoprotein
10. What or how is the lipid peroxidation occur
PROTEIN ELEMENTER & METABOLISM
Abstract
Proteins play an important role in virtually every life process; proteins display a
diverse function such as regulate metabolism (hormones), play a role in gas transport
(hemoglobin), against pathogens (immunoglobulin), etc. Protein consists of amino acids that
are joined together by peptide bonds. Protein has complexity of structures and can be found
in primary, secondary, tertiary and quaternary structure. Amino acids can be classified
based on chemical properties or on nutritional aspect. Amino acids are not stored by our
body. Amino acids are obtained from the diet, synthesized de novo, or produced from
normal protein degradation. Excess of amino acids in our body are rapidly degraded.
Catabolism of amino acids involves: i) the removal of the α-amino groups, forming free
ammonia which is used in the synthesis of urea (urea cycle); this is the important route of
nitrogen disposal, ii) catabolism of carbon skeletons that are converted to common
intermediates of energy production, depending on the type of amino acids.
Mutation of gene generally results in abnormal proteins that may lead to so called inborn
errors of metabolism which most of the diseases are rare. The most important disease of
amino acid metabolism is phenylketonuria (PKU) because it is relatively common and
responds to dietary treatment.
Learning tasks
Udayana University Faculty of Medicine, DME, 2015
5
Study Guide Basic
Biochemistry
1.
2.
3.
4.
5.
6.
What is protein and what is amino acid? What is peptide bond?
Describe and give example of quaternary protein
Describe amino acid classification
Describe the fate of carbon skeletons of amino acids
Describe urea cycle
Describe the underlying cause of PKU, maple syrup urine
homocystinuria, albinism and alkaptonuria
disease,
CARBOHYDRATE METABOLISM
Abstract
The simple forms of carbohydrate and has importance role is glucose. There are
several transporter for glucose to enter the cell. The clinical importance of glucose is to
provide energy for body by glycolysis. Glucose catabolism and generate energy. Excess of
glucose will change in to glycogen and stores in liver and muscle which can turn again in to
glucose.
Glucose also entering pentose pathway “shunt” and produce ribose. It also entering
intermediate metabolism called Tricarboxylic Acid Cycle and produce energy.
Learning Task:
1. Explain what happened during investment stage, splitting stage and yield stage on
glycolisis.
2. How many ATP produced froma aerob glycolysis?
3. Explain about glycogenesis, glycogenolysis and hormonal control of glycogenolysis!
4. Where is Pentosa phosphate pathway started and what are the main products?
Explain why its called “shunt”?
5. How many ATP produced from one molecule glucose metabolized at Kreb’s cycle?
ENZYME
Abstract
Enzymes are specific proteins catalyst. Working of enzymes are affected by many
factors such as; substrate and enzyme concentration, temperature, Acidity (pH), and
inhibitors. Enzymes greatly affect the rate of a reaction and makes the reaction faster with
less energy (enzyme kineticts). Coenzyme is a non-protein compound that helps the
working of enzymes in enzymatic reactions. Enzymes found in almost all reaction or
metabolism in the cells such as; in the digestive system, energy and protein synthesis and
others. Specificity of the enzyme in catalyzes a reaction determined by several factors such
as; geometric shapes of substrate, type of substrate, type of reaction, chemical bond and
functional groups. This specificity will be easier to identify the type or class of enzymes,
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Study Guide Basic
Biochemistry
although not directly able to classify the class of enzymes. IUBS system has clearly can
classify classes of enzymes and until now has been known six classes of enzymes include:
Oxydoreductase, Transferase, Hydrolase, Lyase, Isomerase and Lygase.
Learning Tasks
1. What is enzyme, koenzyme and holoenzyme
2. What is non protein catalyst
3. What is prosthetic groups
4. What is enzyme kinetics
5. Describe the mechanism of enzyme working
6. Describe the function of enzyme in metabolisms reaction.
7. Explain definition and mechanism of competitive inhibitors
8.
What is a non-functional plasma enzyme?. Give five examples
9. Explain about classification of enzyme based on IUBS system.
10. Why digestive enzymes are classified into hydrolase?.
BIOENERGETICS
Abstract
Bioenergetics describes the transfer and utilization of energy in biologic systems. It makes
use of a few basic ideas from the field of thermo-dynamics, particularly the concept of free
energy. Changes in free energy (G) provide a measure of the energetic feasibility of a
chemical reaction and can, therefore, allow prediction of whether a reaction or process can
take place. Bioenergetics concerns only the initial and final energy states of reaction
components, not the mechanism or how much time is needed for the chemical change to
take place. The direction and extent to which a chemical reaction proceeds is determined by
the degree to which two factors change during the reaction. These are enthalpy (H, a
measure of the change in heat content of the reactants and products) and entropy (S, a
measure of the change in randomness or disorder of reactants and products). Enthalpy and
entropy can be used to define a third quantity, free energy (G), which predicts the direction
in which a reaction will spontaneously proceed. The change in free energy is represented in
two ways, G and G0. ΔG represents the change in free energy and, thus, the direction
of a reaction at any specified concentration of products and reactants. This contrasts with
the standard free energy change, G0, which is the energy change when reactants and
products are at a concentration of 1 mol/L.
Learning Task
1. Explain the Thermodynamics Low!
Udayana University Faculty of Medicine, DME, 2015
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Study Guide Basic
Biochemistry
2.
3.
4.
5.
Explain the free energy, enthalpy and entropy concept!
Describe the structure of ATP!
How does ATP as an energy carrier?
What is coupling reaction?
THE ELECTRON TRANSPORT CHAIN & OXIDATIVE PHOSPHORYLATION
Abstract
Energy-rich molecules, such as glucose, are metab olized by a series of oxidation reactions
ultimately yielding CO2 and water. The metabolic intermediates of these reactions donate
electrons to specific coenzymes nicotinamide adenine dinucleotide (NAD+) and flavin
adenine dinucleotide (FAD) to form the energy-rich reduced coenzymes, NADH and FADH2.
These reduced coenzymes can, in turn, each donate a pair of electrons to a specialized set
of electron carriers, collectively called the electron transport chain. As electrons are
passed down the electron transport chain, they lose much of their free energy. Part of this
energy can be captured and stored by the production of ATP from ADP and inorganic
phosphate (Pi). This process is called oxidative phosphorylation. The chemiosmotic
hypothesis (also known as the Mitchell hypothesis) explains how the free energy generated
by the transport of electrons
by the electron transport chain is used to produce ATP from ADP + Pi.
Learning Task
1.
2.
3.
4.
5.
6.
What is Electron Transport Chain?
Discribe the transport of electron on the mitochondrial electron transport system!
What is Oxidative phosphorylation?
Discribe the structure of the ATP sinthase!
Explain The Chemyosmotic Hypothesis of ATP synthesis!
Mention few examples of Inhibitors and uncouplers?
VITAMIN AND MINERAL
Abstract
Vitamins are organic nutrients with essential metabolic functions, generally required
in small amounts in the diet because they cannot be synthesized by the body. The lipidsoluble vitamins (A, D, E, and K) are hydrophobic molecules requiring normal fat absorption for their efficient absorption and the avoidance of deficiency symptoms. Vitamin A
Udayana University Faculty of Medicine, DME, 2015
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Study Guide Basic
Biochemistry
(retinol), present in carnivorous diets, and the provitamin (β-carotene), found in plants, form
retinaldehyde, utilized in vision, and retinoic acid, which acts in the control of gene
expression. Vitamin D is a steroid prohormone yielding the active hormone derivative
calcitriol, which regulates calcium and phosphate metabolism. Vitamin D deficiency leads to
rickets and osteomalacia.
Vitamin E (tocopherol) is the most important antioxidant in the body, acting in the
lipid phase of
membranes and protecting against the effects of free radicals. Vitamin K functions as
cofactor to a carboxylase that acts on glutamate residues of clotting factor precursor
proteins to enable them to chelate calcium. The water-soluble vitamins of the B complex act
as enzyme cofactors. Thiamin is a cofactor in oxidative decarboxylation of α-keto acids and
of transketolase in the pentose phosphate pathway. Riboflavin and niacin are important
cofactors in oxidoreduction reactions, respectively present in flavoprotein enzymes and in
NAD and NADP.
Pantothenic acid is present in coenzyme A and acylcarrier protein, which act as
carriers for acyl groupsin metabolic reactions. Pyridoxine, as pyridoxal phosphate, is the
coenzyme for several enzymes of amino acid metabolism, including the aminotransferases,
and of glycogen phosphorylase. Biotin is the
coenzyme for several carboxylase enzymes. Besides other functions, vitamin B12 and folic
acid take part in providing one-carbon residues for DNA synthesis, deficiency resulting in
megaloblastic anemia. Vitamin C is a water-soluble antioxidant that maintains vitamin E and
many metal cofactors in the reduced state.
Inorganic mineral elements that have a function in the body must be provided in the
diet. When insufficient, deficiency symptoms may arise, and if present in excess they may
be toxic.
FREE RADICAL & ANTI OXIDANT
Abstract
A free radical is an atom or molecule or ion that has a single unpaired electron in an
outer shell. Free radicals are highly reactive and have the potential to cause damage to
cells, including damage that may lead to cancer. Free radicals are formed naturally in the
body. Some free radicals arise normally during metabolism. Sometimes the body immune
system cells purposefully create them to neutralize viruses and bacteria. However,
environmental factors such as pollution, radiation, cigarette smoke and herbicides can also
spawn free radicals. While a few free radicals such as melanin are not chemically reactive,
most biologically-relevant free radicals are highly reactive.
Antioxidants are chemicals that block the activity of free radicals. Normally, the body
can handle free radicals, but if antioxidants are unavailable, or if the free-radical production
becomes excessive, damage can occur that's called oxidative stress. The vitamins C and E,
are thought to protect the body against the destructive effects of free radicals. Antioxidants
neutralize free radicals by donating one of their own electrons, ending the electron-"stealing"
reaction. The antioxidant nutrients themselves do not become free radicals by donating an
electron because they are stable in either form. They act as scavengers, helping to prevent
cell and tissue damage that could lead to cellular damage and disease.
Learning Task
1. What is the diffrece between free radical and oxidant?
2. Classify free radical based on their sources!
3. Explain about chain reaction .
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Biochemistry
4. Give 3 of biological markers to detect oksidatif damage by free radical
5. Give 3 examples of the beneficial of free radical
6. Differentiate between internal and external antioxidant
7. Give some example of external anti oxidant and internal antioxidant
EXTRACELLULAR MATRIX
Abstract
Extra celuler Matrix also called connective tissue, placed in extra cell space. Which
most of it formed from protein. Amount, distribution and component depend on structure and
function. Differentiation of the composition and turnover related to chronic disease.
Learning Task
1. What is ECM?
2. How was the differentiation of ECM?
CASE
A 35-year-old man employee has 90 kg of weight, 165 cm of height and 110 cm of
abdominal circumference. He always has his meals in a canteen next to his office. Food he
eats every day is quite similar. He eats twice a day, at 2pm and 8pm. His daily meals are
described as follows: i) for breakfast, he sometimes drinks instant coffee and eats fried
bananas, ii) for lunch, he always takes rice, crispy-skin fried chicken, fried tofu, fried tempe,
soup of vegetables nodes which contains pumpkin, baby corn, and peanuts, iii) for dinner,
he eats rice with fried or grilled chicken, raw cucumber and basil. He has almost no
exercise/sports because of his busy works. Recently, he complains of fatique and
weakness.
Learning Task SGD 1
1.
2.
3.
4.
5.
6.
Mention and explain content of macronutrient in the case!
Mention and explain the missing nutrients in the case
Are there essential amino acids within the food? Explain!
Mention and explain vitamins content of his meal!
Mention and explain minerals content of his meal!
Mention and explain fibers content of his meal!
Learning Task SGD 2 and 3 will be given later
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Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER
TANGGAL
11 Januari 2016
TEMPAT
Lab. Bersama Lt
WAKTU
08.00-09.00
NIM MAHASISWA
1502005001 s/d
4
Lab. Bersama Lt
09.00-10.00
1502005029
1502005053 s/d
4
Lab. Bersama Lt
10.00-11.00
1502005070
1502005120 s/d
Sutadarma
4
Lab. Bersama Lt
11.00-12.00
1502005144
1502005181 s/d
Sutadarma
4
INSTRUKTUR
Sutadarma dan
Supadmanaba
Sutadarma dan
Supadmanaba
1502005223
Lab Farmasi Lt
08.00-09.00
1502005030 s/d
Dewi Wiryanthini
1
Lab Farmasi Lt
09.00-10.00
1502005051
1502005071 s/d
Dewi Wiryanthini
1
Lab Farmasi Lt
10.00-11.00
1502005118
1502005145 s/d
Dewi Wiryanthini
1
Lab Farmasi Lt
11.00-12.00
1502005178
1502005235 s/d
Dewi Wiryanthini
1
Udayana University Faculty of Medicine, DME, 2015
1502005262
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Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS
TANGGAL
TEMPAT
WAKTU
NIM MAHASISWA
INSTRUKTUR
11 Januari 2016
Lab. Bersama Lt
12.00-13.00
1502005004 s/d
Sutadarma
4
Lab. Bersama Lt
13.00-14.00
1502005033
1502005095 s/d
Sutadarma
4
Lab. Bersama Lt
14.00-15.00
1502005135
1502005172 s/d
Sutadarma
4
Lab. Bersama Lt
15.00-16.00
1502005189
1502005205 s/d
Sutadarma
4
1502005231
Lab Farmasi Lt
12.00-13.00
1502005035 s/d
1
Lab Farmasi Lt
13.00-14.00
1502005094
1502005139 s/d
1
Lab Farmasi Lt
14.00-15.00
1502005171
1502005190 s/d
Dewi Wiryanthini
1
Lab Farmasi Lt
15.00-16.00
1502005204
1502005234 s/d
Dewi Wiryanthini
1
Udayana University Faculty of Medicine, DME, 2015
Dewi Wiryanthini dan
Supadamanaba
Dewi Wiryanthini dan
Supadamanaba
1502005263
12
Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER
TANGGAL
TEMPAT
WAKTU
NIM MAHASISWA
INSTRUKTUR
12 Januari 2016
Lab. Bersama Lt
08.00-09.00
1502005001 s/d
Desak Wihandani
4
Lab. Bersama Lt
09.00-10.00
1502005029
1502005053 s/d
dan Supadmanaba
Desak Wihandani
4
Lab. Bersama Lt
10.00-11.00
1502005070
1502005120 s/d
dan Supadmanaba
Agus Bagiada dan
Supadmanaba
4
Lab. Bersama Lt
11.00-12.00
1502005144
1502005181 s/d
4
Agus Bagiada dan
Supadmanaba
1502005223
Lab Farmasi Lt
08.00-09.00
1502005030 s/d
Tianing
1
Lab Farmasi Lt
09.00-10.00
1502005051
1502005071 s/d
Tianing
1
Lab Farmasi Lt
10.00-11.00
1502005118
1502005145 s/d
Ayu Dewi
1
Lab Farmasi Lt
11.00-12.00
1502005178
1502005235 s/d
Ayu Dewi
1
Udayana University Faculty of Medicine, DME, 2015
1502005262
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Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS
TANGGAL
12 Januari 2016
TEMPAT
Lab. Bersama Lt
WAKTU
12.00-13.00
NIM MAHASISWA
1502005004 s/d
INSTRUKTUR
Surudarma
4
Lab. Bersama Lt
13.00-14.00
1502005033
1502005095 s/d
Surudarma
4
Lab. Bersama Lt
14.00-15.00
1502005135
1502005172 s/d
Tianing
4
Lab. Bersama Lt
15.00-16.00
1502005189
1502005205 s/d
Tianing
4
1502005231
Lab Farmasi Lt
12.00-13.00
1502005035 s/d
1
Lab Farmasi Lt
13.00-14.00
1502005094
1502005139 s/d
1
Lab Farmasi Lt
14.00-15.00
1502005171
1502005190 s/d
Ayu Dewi
1
Lab Farmasi Lt
15.00-16.00
1502005204
1502005234 s/d
Ayu Dewi
1
Udayana University Faculty of Medicine, DME, 2015
Agus Bagiada dan
Supadmanaba
Agus Bagiada dan
Supadmanaba
1502005263
14
Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER
TANGGAL
13 Januari 2016
TEMPAT
Lab. Bersama Lt
WAKTU
08.00-09.00
NIM MAHASISWA
1502005001 s/d
4
Lab. Bersama Lt
09.00-10.00
1502005029
1502005053 s/d
4
Lab. Bersama Lt
10.00-11.00
1502005070
1502005120 s/d
Ayu Dewi
4
Lab. Bersama Lt
11.00-12.00
1502005144
1502005181 s/d
Ayu Dewi
4
INSTRUKTUR
Agus Bagiada dan
Supadmanaba
Agus Bagiada dan
Supadmanaba
1502005223
Lab Farmasi Lt
08.00-09.00
1502005030 s/d
Desak Wihandani
1
Lab Farmasi Lt
09.00-10.00
1502005051
1502005071 s/d
Desak Wihandani
1
Lab Farmasi Lt
10.00-11.00
1502005118
1502005145 s/d
Desak Wihandani
1
Lab Farmasi Lt
11.00-12.00
1502005178
1502005235 s/d
Surudarma
1
1502005262
JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS
TANGGAL
13 Januari 2016
TEMPAT
Lab. Bersama Lt
WAKTU
12.00-13.00
NIM MAHASISWA
1502005004 s/d
INSTRUKTUR
Surudarma
4
Lab. Bersama Lt
13.00-14.00
1502005033
1502005095 s/d
Ayu Dewi
4
Lab. Bersama Lt
14.00-15.00
1502005135
1502005172 s/d
Surudarma
4
Lab. Bersama Lt
15.00-16.00
1502005189
1502005205 s/d
Surudarma
4
Udayana University Faculty of Medicine, DME, 2015
1502005231
15
Study Guide Basic
Biochemistry
Lab Farmasi Lt
12.00-13.00
1502005035 s/d
Tianing
1
Lab Farmasi Lt
13.00-14.00
1502005094
1502005139 s/d
Tianing
1
Lab Farmasi Lt
14.00-15.00
1502005171
1502005190 s/d
1
Lab Farmasi Lt
15.00-16.00
1502005204
1502005234 s/d
1
Desak Wihandani
dan Supadmanaba
Desak Wihandani
dan Supadmanaba
1502005263
Catatan:
Mbak Amy bertugas pagi di Lab lantai 4, siang di Lab lantai 1
CURRICULUM MAP
Smstr
10
9
8
7
6
5
4
Health Systembased Practice
(3 weeks)
BCS (1 weeks)
The Cardiovascular
System and
Disorders
(3 weeks)
BCS (1 weeks)
Neuroscience and
neurological
disorders
(3 weeks)
BCS (1 weeks)
Musculoskeletal
system &
Program or curriculum blocks
Senior Clerkship
Senior Clerkship
Senior Clerkship
Community-based
Evidence-based
Elective Study IV
practice
Medical Practice
(evaluation)
(4 weeks)
(2 weeks)
Special topics :
(3 weeks)
Health
Ergonomic &
Health
Environment
(2 weeks)
Medical Emergency
The Urinary
The Reproductive
(3 weeks)
System and
System and Disorders
Disorders
(4 weeks)
(3 weeks)
BCS (1 weeks)
BCS (1 weeks)
BCS (1 weeks)
The Respiratory System
The skin & hearing Special Topic :
and Disorders
system
- Palliative med
(4 weeks)
& disorders
- Complemnt &
(3 weeks)
Alternative Med.
BCS (1 weeks)
- Forensic
BCS (1 weeks)
(3 weeks)
Alimentary
The Endocrine
Clinical Nutrition and
& hepatobiliary systems
System,
Disorders
Udayana University Faculty of Medicine, DME, 2015
Comprehensi
ve Clinic
Orientation
(Clerkship)
+ medical
ethic
(4 weeks)
19 weeks
Elective
Study III
19 weeks
(3 weeks)
Elective
Study II
(2 weeks)
18 weeks
The Visual
system &
19 weeks
16
Study Guide Basic
Biochemistry
3
2
1
connective tissue
disorders
(3 weeks)
BCS (1 weeks)
Basic microbiology
& parasitology
(3 weeks)
Basic Infection
& infectious
diseases
(3 weeks)
BCS (1 weeks)
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communication
(3 weeks)
Basic pharmacology
(2 weeks)
BCS (1 weeks)
Studium
Generale
and
Humaniora
(2 weeks)
Basic
Anatomy
( 4 weeks)
& disorders
(3 Weeks)
Metabolism and
Disorders
(4 weeks)
BCS (1 weeks)
Hematologic
system & disorder
& clinical
oncology
(3 weeks)
BCS (1 weeks)
(2 weeks)
Medical
Professionalism
(2 weeks) + medical
ethic (1 weeks)
Basic Anatomy
Pathology & Clinical
pathology (3 weeks)
BCS (1 weeks)
Behavior Change
and disorders
(3 weeks)
Elective Study I
(2 weeks)
The cell
as biochemical
machinery
(2 weeks)
Basic
Histology
(2 weeks) &
Basic
Physiology
(3 weeks)
BCS (1
weeks)
Growth &
developme
nt
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ry
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weeks)
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disorders
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drug etics
19 weeks
(1 weeks)
19 weeks
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19
weeks
Pendidikan Pancasila & Kewarganegaraan ( 3 weeks )
Inter Professional Education (smt 3-7)
Udayana University Faculty of Medicine, DME, 2015
17
Biochemistry
PLANNERS TEAM
No.
NAME
PHONE
1.
Dr.dr. Desak Made Wihandani, M.Kes
Head
081338776244
2.
Dr.ret.nat.dr. Ni Nyoman Ayu Dewi
Secretary
081337141506
3.
Prof.dr. I Nyoman Agus Bagiada,
SpBiok
Member
081338338611
4.
dr. I Wayan Surudarma, M.Si
Member
081338486589
5.
dr. I Wayan Gede Sutadarma, M.Gizi,
SpGK
Member
087862155380
6.
dr. Ida Ayu
M.Biomed
7
Dr. Ni Wayan Tianing, SSi, M.Kes
Dewi
Wiryanthini, Member
Udayana University Faculty of Medicine, DME, 2015
Member
08123625239
08123982504
1
Study Guide Basic
Biochemistry
~FACILITATORS ~
NO
GROUP
DEPT
PHONE
VENUE
1
Radiology
081805673099
2
Dr.dr. Elysanti Dwi Martadiani,
Sp.Rad
dr. Reni Widyastuti, S.Ked
2
Pharmacology
08174742501
3
dr. Ni Ketut Putri Ariani, Sp.KJ
3
Psychiatry
082237817384
4
dr I Gusti Agung Gede Utara
Hartawan, Sp.An, MARS
dr. Ni Luh Ariwati
4
Anasthesi
08123868126
5
Parasitology
08123662311
6
Histology
08124665966
7
Microbiology
08553711398
8
dr. I G Kamasan Nyoman
Arijana, M.Si, Med
Dr.dr. Ni Nyoman Sri
Budayanti, Sp.MK(K)
dr. Ni Nyoman Mahartini, Sp.PK
8
081337165577
9
dr. I Wayan Sugiritama, M.Kes
9
Clinical
Pathology
Histology
10
dr. Ryan Saktika Mulyana,
M.Biomed, Sp.OG
10
Obgyn
082147087905
2nd floor:
R.2.01
2nd floor:
R.2.02
2nd floor:
R.2.03
2nd floor:
R.2.04
2nd floor:
R.2.05
2nd floor:
R.2.06
2nd floor:
R.2.07
2nd floor:
R.2.08
2nd floor:
R.2.21
2nd floor:
R.2.22
GROUP
1
DEPT
Forensic
PHONE
081338472005
2
Pediatri
081353027973
3
dr. I Nyoman Budi Hartawan,
M.Sc., Sp.A(K)
dr. I Wayan Surudarma, M.Si
3
Biochemistry
081338486589
4
dr. I Gusti Ayu Artini, M.Sc
4
Pharmacology
08123650481
5
dr. I Ketut Mariadi, Sp.PD
5
Interna
08123853700
6
Dr.dr. Ni Made Linawati, M.Si
6
Histology
081337222567
7
dr. I Nyoman Gede Wardana, M
Biomed
dr. I Wyn Subawa, Sp.OT
7
Anatomy
087860405625
8
Orthopaedy
Dr.rer.Nat. dr. Ni Nyoman Ayu
Dewi, M.Kes
dr. I Komang Arimbawa, Sp.S
9
Biochemistry
081338913087
081337096388
081337141506
10
Neurology
081338226892
1
5
6
7
NAME
08164732743
ENGLISH CLASS
NO
1
2
8
9
10
NAME
dr. Kunthi Yulianti, Sp.KF
Udayana University Faculty of Medicine, DME, 2015
VENUE
2nd floor:
R.2.01
2nd floor:
R.2.02
2nd floor:
R.2.03
2nd floor:
R.2.04
2nd floor:
R.2.05
2nd floor:
R.2.06
2nd floor:
R.2.07
2nd floor:
R.2.08
2nd floor:
R.2.21
2nd floor:
R.2.22
2
Study Guide Basic
Biochemistry
TIME TABLE BLOCK BASIC BIOCHEMISTRY (Dec, 28, 2015 - Jan, 15, 2016)
Day
Date
1
Monday,
Dec,
28,
2015
2
Tue, Dec,
29, 2015
Topic
Introduction
Biochemistry
Elementer
Carbohydrate
Learning
situation
to
Elementer Lipid
Elementer Protein
Protein metabolism
3
4
Wed, Dec,
30, 2015
Thursday,
Dec,31,
2015
Carbohydrate
Metabolism 1
Carbohydrate
Metabolism 2
Lipid metabolism 1
Lipid Metabolism 2
5
Mon, Jan,
4, 2016
6
Tue, Jan, 5,
2016
7
8
Wed, Jan,
6, 2016
Thu, Jan, 7,
2016
Intermetabolism
relationship
Enzyme
Bioenergetics
Phosphorylation
Oxydation
Vitamin and Mineral
Free Radical & Anti
oxidant
Matrix extracelular
Panel Discussion
9
Mon, Jan,
11, 2016
SGD & Practicum 1
10
Tue,
Jan,
12, 2016
SGD & Practicum 2
11
Wed, Jan,
13, 2016
SGD & Practicum 3
English
Class
Regular
Class
Lecture Intro
IL & L Task
Lecture 1
IL & L Task
Break
Lecture 2
Lecture 7
IL & L task
Break
Lecture 8
IL & L task
Lecture 3
IL & L task
Break
Lecture 4
IL & L task
Lecture 5
IL & L task
Break
Lecture 6
IL & L task
Lecture 9
IL & L task
Break
Lecture 10
IL & L task
Lecture 13
IL & L task
Break
Lecture 14
IL & L task
Lecture 11
IL & L task
Break
Lecture 12
IL & L task
Lecture 15
IL & L task
Plenary
08.00-09.00
09.00-10.30
10.30-11.30
11.30-13.00
13.00-14.00
14.00-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-11.30
11.30-12.30
12.30-13.30
13.30-15.00
08.00-09.00
09.00-10.00
10.00-12.00
09.00-10.00
10.00-11.30
11.30-12.30
13.30-15.00
12.30-13.30
15.00-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-12.30
12.30-13.30
13.30-14.30
14.30-16.00
09.00-10.00
10.00-11.00
12.00-14.00
SGD 1
Break
Practicum
Glucose
SGD 2
Break
Practicum Protein
SGD 3
Break
Practicum
Enzyme
08.00-10.00
10.00-11.00
11.00-15.00
13.00-15.00
12.00-13.00
08-00-12.00
08.00-10.00
10.00-11.00
11.00-15.00
08.00-10.00
10.00-11.00
11.00-15.00
13.00-15.00
12.00-13.00
08-00-12.00
13.00-15.00
12.00-13.00
08-00-12.00
Udayana University Faculty of Medicine, DME, 2015
PIC
Bagiada
Sutadarma
Sutadarma
Ayu Dewi
Ayu Dewi
Dewi
Wiryanthini
Dewi
Wiryanthini
Bagiada
Bagiada
Bagiada
Tianing
Surudarma
Surudarma
Sutadarma
Desak
Dewi
Wiryanthini
Team
Team &
Fasilitator
Team &
Fasilitator
Team &
Fasilitator
3
Study Guide Basic
Biochemistry
12
13
Thu,
Jan,
14, 2016
Friday,
Jan,15,
2016
Silent Day
Evaluation
Team
CARBOHYDRATE ELEMENTER
Abstract
Carbohydrates are major constituents of animal food and animal tissues. They are
characterized by the type and number of monosaccharide residues in their molecules.
Glucose is the most important carbohydrate in mammalian biochemistry because nearly all
carbohydrate in food is converted to glucose for metabolism. Sugars have large numbers of
stereoisomers because they contain several asymmetric carbon atoms. The
monosaccharides include glucose, the “blood sugar”; and ribose, an important constituent of
nucleotides and nucleic acids.
The disaccharides include maltose (glucosyl glucose), an intermediate in the
digestion of starch; sucrose (glucosyl fructose), important as a dietary constituent containing
fructose; and lactose (galactosyl glucose), in milk. Starch and glycogen are storage
polymers of glucose in plants and animals, respectively. Starch is the major source of
energy in the diet.
Complex carbohydrates contain other sugar derivatives such as amino sugars,
uronic acids, and sialic acids. They include proteoglycans and glycosaminoglycans,
associated with structural elements of the tis-sues; and glycoproteins, proteins containing
attached oligosaccharide chains. They are found in many situations including the cell
membrane.
Learning Task
1. Describes the characteristic of glucose, fructose and galactose
2. Describes the classification of carbohydrate
3. Identify the food sources of each carbohydrate
4. Describes the isomerism of glucose
5. Describes the characteristic of hexose and pentose sugar
6. Why the cell usually use glucose as a fuel
7. Describe the characteristic of glycogen and starch
8. Describes the characteristic of carbohydrate as a fiber
LIPID ELEMENTER
Abstract
Lipids have the common property of being relatively insoluble in water (hydrophobic)
but soluble in non-polar solvents. Amphipathic lipids also contain one or more polar groups,
making them suitable as constituents of membranes at lipid : water interfaces. The lipids of
major physiologic significance are fatty acids and their esters, together with cholesterol and
other steroids.
Long-chain fatty acids may be saturated, monounsaturated, or polyunsaturated,
according to the number of double bonds present. Their fluidity decreases with chain length
and increases according to degree of unsaturation. Eicosanoids are formed from 20-carbon
polyunsaturated fatty acids and make up an important group of physiologically and
Udayana University Faculty of Medicine, DME, 2015
4
Study Guide Basic
Biochemistry
pharmacologically active compounds known as prostaglandins, thromboxanes, leukotrienes,
and lipoxins.
The esters of glycerol are quantitatively the most significant lipids, represented by
triacylglycerol (“fat”), a major constituent of lipoproteins and the storage form of lipid in
adipose tissue. Phosphoacylglycerols are amphipathic lipids and have important roles—as
major constituents of membranes and the outer layer of lipoproteins, as surfactant in the
lung, as precursors of second messengers, and as constituents of nervous tissue.
Glycolipids are also important constituents of nervous tissue such as brain and the outer
leaflet of the cell membrane, where they contribute to the carbo-hydrates on the cell
surface.
Cholesterol, an amphipathic lipid, is an important component of membranes. It is the
parent molecule from which all other steroids in the body, including major hormones such as
the adrenocortical and sex hormones, D vitamins, and bile acids, are synthesized.
Peroxidation of lipids containing polyunsaturated fatty acids leads to generation of free
radicals that may damage tissues and cause disease.
Learning Task
1. Describes the characteristic of lipid
2. Describes the classification of lipid
3. Identify the nomenclature methods of lipid
4. Describes the different between saturated fatty acids and unsaturated fatty acids
5. Identify the food sources of each fatty acids
6. Describes the characteristic of essential fatty acids
7. Describes the different between cis- and trans- fatty acids
8. Describes the characteristic of cholesterol
9. Describe the characteristic of lipoprotein
10. What or how is the lipid peroxidation occur
PROTEIN ELEMENTER & METABOLISM
Abstract
Proteins play an important role in virtually every life process; proteins display a
diverse function such as regulate metabolism (hormones), play a role in gas transport
(hemoglobin), against pathogens (immunoglobulin), etc. Protein consists of amino acids that
are joined together by peptide bonds. Protein has complexity of structures and can be found
in primary, secondary, tertiary and quaternary structure. Amino acids can be classified
based on chemical properties or on nutritional aspect. Amino acids are not stored by our
body. Amino acids are obtained from the diet, synthesized de novo, or produced from
normal protein degradation. Excess of amino acids in our body are rapidly degraded.
Catabolism of amino acids involves: i) the removal of the α-amino groups, forming free
ammonia which is used in the synthesis of urea (urea cycle); this is the important route of
nitrogen disposal, ii) catabolism of carbon skeletons that are converted to common
intermediates of energy production, depending on the type of amino acids.
Mutation of gene generally results in abnormal proteins that may lead to so called inborn
errors of metabolism which most of the diseases are rare. The most important disease of
amino acid metabolism is phenylketonuria (PKU) because it is relatively common and
responds to dietary treatment.
Learning tasks
Udayana University Faculty of Medicine, DME, 2015
5
Study Guide Basic
Biochemistry
1.
2.
3.
4.
5.
6.
What is protein and what is amino acid? What is peptide bond?
Describe and give example of quaternary protein
Describe amino acid classification
Describe the fate of carbon skeletons of amino acids
Describe urea cycle
Describe the underlying cause of PKU, maple syrup urine
homocystinuria, albinism and alkaptonuria
disease,
CARBOHYDRATE METABOLISM
Abstract
The simple forms of carbohydrate and has importance role is glucose. There are
several transporter for glucose to enter the cell. The clinical importance of glucose is to
provide energy for body by glycolysis. Glucose catabolism and generate energy. Excess of
glucose will change in to glycogen and stores in liver and muscle which can turn again in to
glucose.
Glucose also entering pentose pathway “shunt” and produce ribose. It also entering
intermediate metabolism called Tricarboxylic Acid Cycle and produce energy.
Learning Task:
1. Explain what happened during investment stage, splitting stage and yield stage on
glycolisis.
2. How many ATP produced froma aerob glycolysis?
3. Explain about glycogenesis, glycogenolysis and hormonal control of glycogenolysis!
4. Where is Pentosa phosphate pathway started and what are the main products?
Explain why its called “shunt”?
5. How many ATP produced from one molecule glucose metabolized at Kreb’s cycle?
ENZYME
Abstract
Enzymes are specific proteins catalyst. Working of enzymes are affected by many
factors such as; substrate and enzyme concentration, temperature, Acidity (pH), and
inhibitors. Enzymes greatly affect the rate of a reaction and makes the reaction faster with
less energy (enzyme kineticts). Coenzyme is a non-protein compound that helps the
working of enzymes in enzymatic reactions. Enzymes found in almost all reaction or
metabolism in the cells such as; in the digestive system, energy and protein synthesis and
others. Specificity of the enzyme in catalyzes a reaction determined by several factors such
as; geometric shapes of substrate, type of substrate, type of reaction, chemical bond and
functional groups. This specificity will be easier to identify the type or class of enzymes,
Udayana University Faculty of Medicine, DME, 2015
6
Study Guide Basic
Biochemistry
although not directly able to classify the class of enzymes. IUBS system has clearly can
classify classes of enzymes and until now has been known six classes of enzymes include:
Oxydoreductase, Transferase, Hydrolase, Lyase, Isomerase and Lygase.
Learning Tasks
1. What is enzyme, koenzyme and holoenzyme
2. What is non protein catalyst
3. What is prosthetic groups
4. What is enzyme kinetics
5. Describe the mechanism of enzyme working
6. Describe the function of enzyme in metabolisms reaction.
7. Explain definition and mechanism of competitive inhibitors
8.
What is a non-functional plasma enzyme?. Give five examples
9. Explain about classification of enzyme based on IUBS system.
10. Why digestive enzymes are classified into hydrolase?.
BIOENERGETICS
Abstract
Bioenergetics describes the transfer and utilization of energy in biologic systems. It makes
use of a few basic ideas from the field of thermo-dynamics, particularly the concept of free
energy. Changes in free energy (G) provide a measure of the energetic feasibility of a
chemical reaction and can, therefore, allow prediction of whether a reaction or process can
take place. Bioenergetics concerns only the initial and final energy states of reaction
components, not the mechanism or how much time is needed for the chemical change to
take place. The direction and extent to which a chemical reaction proceeds is determined by
the degree to which two factors change during the reaction. These are enthalpy (H, a
measure of the change in heat content of the reactants and products) and entropy (S, a
measure of the change in randomness or disorder of reactants and products). Enthalpy and
entropy can be used to define a third quantity, free energy (G), which predicts the direction
in which a reaction will spontaneously proceed. The change in free energy is represented in
two ways, G and G0. ΔG represents the change in free energy and, thus, the direction
of a reaction at any specified concentration of products and reactants. This contrasts with
the standard free energy change, G0, which is the energy change when reactants and
products are at a concentration of 1 mol/L.
Learning Task
1. Explain the Thermodynamics Low!
Udayana University Faculty of Medicine, DME, 2015
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Biochemistry
2.
3.
4.
5.
Explain the free energy, enthalpy and entropy concept!
Describe the structure of ATP!
How does ATP as an energy carrier?
What is coupling reaction?
THE ELECTRON TRANSPORT CHAIN & OXIDATIVE PHOSPHORYLATION
Abstract
Energy-rich molecules, such as glucose, are metab olized by a series of oxidation reactions
ultimately yielding CO2 and water. The metabolic intermediates of these reactions donate
electrons to specific coenzymes nicotinamide adenine dinucleotide (NAD+) and flavin
adenine dinucleotide (FAD) to form the energy-rich reduced coenzymes, NADH and FADH2.
These reduced coenzymes can, in turn, each donate a pair of electrons to a specialized set
of electron carriers, collectively called the electron transport chain. As electrons are
passed down the electron transport chain, they lose much of their free energy. Part of this
energy can be captured and stored by the production of ATP from ADP and inorganic
phosphate (Pi). This process is called oxidative phosphorylation. The chemiosmotic
hypothesis (also known as the Mitchell hypothesis) explains how the free energy generated
by the transport of electrons
by the electron transport chain is used to produce ATP from ADP + Pi.
Learning Task
1.
2.
3.
4.
5.
6.
What is Electron Transport Chain?
Discribe the transport of electron on the mitochondrial electron transport system!
What is Oxidative phosphorylation?
Discribe the structure of the ATP sinthase!
Explain The Chemyosmotic Hypothesis of ATP synthesis!
Mention few examples of Inhibitors and uncouplers?
VITAMIN AND MINERAL
Abstract
Vitamins are organic nutrients with essential metabolic functions, generally required
in small amounts in the diet because they cannot be synthesized by the body. The lipidsoluble vitamins (A, D, E, and K) are hydrophobic molecules requiring normal fat absorption for their efficient absorption and the avoidance of deficiency symptoms. Vitamin A
Udayana University Faculty of Medicine, DME, 2015
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Study Guide Basic
Biochemistry
(retinol), present in carnivorous diets, and the provitamin (β-carotene), found in plants, form
retinaldehyde, utilized in vision, and retinoic acid, which acts in the control of gene
expression. Vitamin D is a steroid prohormone yielding the active hormone derivative
calcitriol, which regulates calcium and phosphate metabolism. Vitamin D deficiency leads to
rickets and osteomalacia.
Vitamin E (tocopherol) is the most important antioxidant in the body, acting in the
lipid phase of
membranes and protecting against the effects of free radicals. Vitamin K functions as
cofactor to a carboxylase that acts on glutamate residues of clotting factor precursor
proteins to enable them to chelate calcium. The water-soluble vitamins of the B complex act
as enzyme cofactors. Thiamin is a cofactor in oxidative decarboxylation of α-keto acids and
of transketolase in the pentose phosphate pathway. Riboflavin and niacin are important
cofactors in oxidoreduction reactions, respectively present in flavoprotein enzymes and in
NAD and NADP.
Pantothenic acid is present in coenzyme A and acylcarrier protein, which act as
carriers for acyl groupsin metabolic reactions. Pyridoxine, as pyridoxal phosphate, is the
coenzyme for several enzymes of amino acid metabolism, including the aminotransferases,
and of glycogen phosphorylase. Biotin is the
coenzyme for several carboxylase enzymes. Besides other functions, vitamin B12 and folic
acid take part in providing one-carbon residues for DNA synthesis, deficiency resulting in
megaloblastic anemia. Vitamin C is a water-soluble antioxidant that maintains vitamin E and
many metal cofactors in the reduced state.
Inorganic mineral elements that have a function in the body must be provided in the
diet. When insufficient, deficiency symptoms may arise, and if present in excess they may
be toxic.
FREE RADICAL & ANTI OXIDANT
Abstract
A free radical is an atom or molecule or ion that has a single unpaired electron in an
outer shell. Free radicals are highly reactive and have the potential to cause damage to
cells, including damage that may lead to cancer. Free radicals are formed naturally in the
body. Some free radicals arise normally during metabolism. Sometimes the body immune
system cells purposefully create them to neutralize viruses and bacteria. However,
environmental factors such as pollution, radiation, cigarette smoke and herbicides can also
spawn free radicals. While a few free radicals such as melanin are not chemically reactive,
most biologically-relevant free radicals are highly reactive.
Antioxidants are chemicals that block the activity of free radicals. Normally, the body
can handle free radicals, but if antioxidants are unavailable, or if the free-radical production
becomes excessive, damage can occur that's called oxidative stress. The vitamins C and E,
are thought to protect the body against the destructive effects of free radicals. Antioxidants
neutralize free radicals by donating one of their own electrons, ending the electron-"stealing"
reaction. The antioxidant nutrients themselves do not become free radicals by donating an
electron because they are stable in either form. They act as scavengers, helping to prevent
cell and tissue damage that could lead to cellular damage and disease.
Learning Task
1. What is the diffrece between free radical and oxidant?
2. Classify free radical based on their sources!
3. Explain about chain reaction .
Udayana University Faculty of Medicine, DME, 2015
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Study Guide Basic
Biochemistry
4. Give 3 of biological markers to detect oksidatif damage by free radical
5. Give 3 examples of the beneficial of free radical
6. Differentiate between internal and external antioxidant
7. Give some example of external anti oxidant and internal antioxidant
EXTRACELLULAR MATRIX
Abstract
Extra celuler Matrix also called connective tissue, placed in extra cell space. Which
most of it formed from protein. Amount, distribution and component depend on structure and
function. Differentiation of the composition and turnover related to chronic disease.
Learning Task
1. What is ECM?
2. How was the differentiation of ECM?
CASE
A 35-year-old man employee has 90 kg of weight, 165 cm of height and 110 cm of
abdominal circumference. He always has his meals in a canteen next to his office. Food he
eats every day is quite similar. He eats twice a day, at 2pm and 8pm. His daily meals are
described as follows: i) for breakfast, he sometimes drinks instant coffee and eats fried
bananas, ii) for lunch, he always takes rice, crispy-skin fried chicken, fried tofu, fried tempe,
soup of vegetables nodes which contains pumpkin, baby corn, and peanuts, iii) for dinner,
he eats rice with fried or grilled chicken, raw cucumber and basil. He has almost no
exercise/sports because of his busy works. Recently, he complains of fatique and
weakness.
Learning Task SGD 1
1.
2.
3.
4.
5.
6.
Mention and explain content of macronutrient in the case!
Mention and explain the missing nutrients in the case
Are there essential amino acids within the food? Explain!
Mention and explain vitamins content of his meal!
Mention and explain minerals content of his meal!
Mention and explain fibers content of his meal!
Learning Task SGD 2 and 3 will be given later
Udayana University Faculty of Medicine, DME, 2015
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Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER
TANGGAL
11 Januari 2016
TEMPAT
Lab. Bersama Lt
WAKTU
08.00-09.00
NIM MAHASISWA
1502005001 s/d
4
Lab. Bersama Lt
09.00-10.00
1502005029
1502005053 s/d
4
Lab. Bersama Lt
10.00-11.00
1502005070
1502005120 s/d
Sutadarma
4
Lab. Bersama Lt
11.00-12.00
1502005144
1502005181 s/d
Sutadarma
4
INSTRUKTUR
Sutadarma dan
Supadmanaba
Sutadarma dan
Supadmanaba
1502005223
Lab Farmasi Lt
08.00-09.00
1502005030 s/d
Dewi Wiryanthini
1
Lab Farmasi Lt
09.00-10.00
1502005051
1502005071 s/d
Dewi Wiryanthini
1
Lab Farmasi Lt
10.00-11.00
1502005118
1502005145 s/d
Dewi Wiryanthini
1
Lab Farmasi Lt
11.00-12.00
1502005178
1502005235 s/d
Dewi Wiryanthini
1
Udayana University Faculty of Medicine, DME, 2015
1502005262
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Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS
TANGGAL
TEMPAT
WAKTU
NIM MAHASISWA
INSTRUKTUR
11 Januari 2016
Lab. Bersama Lt
12.00-13.00
1502005004 s/d
Sutadarma
4
Lab. Bersama Lt
13.00-14.00
1502005033
1502005095 s/d
Sutadarma
4
Lab. Bersama Lt
14.00-15.00
1502005135
1502005172 s/d
Sutadarma
4
Lab. Bersama Lt
15.00-16.00
1502005189
1502005205 s/d
Sutadarma
4
1502005231
Lab Farmasi Lt
12.00-13.00
1502005035 s/d
1
Lab Farmasi Lt
13.00-14.00
1502005094
1502005139 s/d
1
Lab Farmasi Lt
14.00-15.00
1502005171
1502005190 s/d
Dewi Wiryanthini
1
Lab Farmasi Lt
15.00-16.00
1502005204
1502005234 s/d
Dewi Wiryanthini
1
Udayana University Faculty of Medicine, DME, 2015
Dewi Wiryanthini dan
Supadamanaba
Dewi Wiryanthini dan
Supadamanaba
1502005263
12
Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER
TANGGAL
TEMPAT
WAKTU
NIM MAHASISWA
INSTRUKTUR
12 Januari 2016
Lab. Bersama Lt
08.00-09.00
1502005001 s/d
Desak Wihandani
4
Lab. Bersama Lt
09.00-10.00
1502005029
1502005053 s/d
dan Supadmanaba
Desak Wihandani
4
Lab. Bersama Lt
10.00-11.00
1502005070
1502005120 s/d
dan Supadmanaba
Agus Bagiada dan
Supadmanaba
4
Lab. Bersama Lt
11.00-12.00
1502005144
1502005181 s/d
4
Agus Bagiada dan
Supadmanaba
1502005223
Lab Farmasi Lt
08.00-09.00
1502005030 s/d
Tianing
1
Lab Farmasi Lt
09.00-10.00
1502005051
1502005071 s/d
Tianing
1
Lab Farmasi Lt
10.00-11.00
1502005118
1502005145 s/d
Ayu Dewi
1
Lab Farmasi Lt
11.00-12.00
1502005178
1502005235 s/d
Ayu Dewi
1
Udayana University Faculty of Medicine, DME, 2015
1502005262
13
Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS
TANGGAL
12 Januari 2016
TEMPAT
Lab. Bersama Lt
WAKTU
12.00-13.00
NIM MAHASISWA
1502005004 s/d
INSTRUKTUR
Surudarma
4
Lab. Bersama Lt
13.00-14.00
1502005033
1502005095 s/d
Surudarma
4
Lab. Bersama Lt
14.00-15.00
1502005135
1502005172 s/d
Tianing
4
Lab. Bersama Lt
15.00-16.00
1502005189
1502005205 s/d
Tianing
4
1502005231
Lab Farmasi Lt
12.00-13.00
1502005035 s/d
1
Lab Farmasi Lt
13.00-14.00
1502005094
1502005139 s/d
1
Lab Farmasi Lt
14.00-15.00
1502005171
1502005190 s/d
Ayu Dewi
1
Lab Farmasi Lt
15.00-16.00
1502005204
1502005234 s/d
Ayu Dewi
1
Udayana University Faculty of Medicine, DME, 2015
Agus Bagiada dan
Supadmanaba
Agus Bagiada dan
Supadmanaba
1502005263
14
Study Guide Basic
Biochemistry
JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER
TANGGAL
13 Januari 2016
TEMPAT
Lab. Bersama Lt
WAKTU
08.00-09.00
NIM MAHASISWA
1502005001 s/d
4
Lab. Bersama Lt
09.00-10.00
1502005029
1502005053 s/d
4
Lab. Bersama Lt
10.00-11.00
1502005070
1502005120 s/d
Ayu Dewi
4
Lab. Bersama Lt
11.00-12.00
1502005144
1502005181 s/d
Ayu Dewi
4
INSTRUKTUR
Agus Bagiada dan
Supadmanaba
Agus Bagiada dan
Supadmanaba
1502005223
Lab Farmasi Lt
08.00-09.00
1502005030 s/d
Desak Wihandani
1
Lab Farmasi Lt
09.00-10.00
1502005051
1502005071 s/d
Desak Wihandani
1
Lab Farmasi Lt
10.00-11.00
1502005118
1502005145 s/d
Desak Wihandani
1
Lab Farmasi Lt
11.00-12.00
1502005178
1502005235 s/d
Surudarma
1
1502005262
JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS
TANGGAL
13 Januari 2016
TEMPAT
Lab. Bersama Lt
WAKTU
12.00-13.00
NIM MAHASISWA
1502005004 s/d
INSTRUKTUR
Surudarma
4
Lab. Bersama Lt
13.00-14.00
1502005033
1502005095 s/d
Ayu Dewi
4
Lab. Bersama Lt
14.00-15.00
1502005135
1502005172 s/d
Surudarma
4
Lab. Bersama Lt
15.00-16.00
1502005189
1502005205 s/d
Surudarma
4
Udayana University Faculty of Medicine, DME, 2015
1502005231
15
Study Guide Basic
Biochemistry
Lab Farmasi Lt
12.00-13.00
1502005035 s/d
Tianing
1
Lab Farmasi Lt
13.00-14.00
1502005094
1502005139 s/d
Tianing
1
Lab Farmasi Lt
14.00-15.00
1502005171
1502005190 s/d
1
Lab Farmasi Lt
15.00-16.00
1502005204
1502005234 s/d
1
Desak Wihandani
dan Supadmanaba
Desak Wihandani
dan Supadmanaba
1502005263
Catatan:
Mbak Amy bertugas pagi di Lab lantai 4, siang di Lab lantai 1
CURRICULUM MAP
Smstr
10
9
8
7
6
5
4
Health Systembased Practice
(3 weeks)
BCS (1 weeks)
The Cardiovascular
System and
Disorders
(3 weeks)
BCS (1 weeks)
Neuroscience and
neurological
disorders
(3 weeks)
BCS (1 weeks)
Musculoskeletal
system &
Program or curriculum blocks
Senior Clerkship
Senior Clerkship
Senior Clerkship
Community-based
Evidence-based
Elective Study IV
practice
Medical Practice
(evaluation)
(4 weeks)
(2 weeks)
Special topics :
(3 weeks)
Health
Ergonomic &
Health
Environment
(2 weeks)
Medical Emergency
The Urinary
The Reproductive
(3 weeks)
System and
System and Disorders
Disorders
(4 weeks)
(3 weeks)
BCS (1 weeks)
BCS (1 weeks)
BCS (1 weeks)
The Respiratory System
The skin & hearing Special Topic :
and Disorders
system
- Palliative med
(4 weeks)
& disorders
- Complemnt &
(3 weeks)
Alternative Med.
BCS (1 weeks)
- Forensic
BCS (1 weeks)
(3 weeks)
Alimentary
The Endocrine
Clinical Nutrition and
& hepatobiliary systems
System,
Disorders
Udayana University Faculty of Medicine, DME, 2015
Comprehensi
ve Clinic
Orientation
(Clerkship)
+ medical
ethic
(4 weeks)
19 weeks
Elective
Study III
19 weeks
(3 weeks)
Elective
Study II
(2 weeks)
18 weeks
The Visual
system &
19 weeks
16
Study Guide Basic
Biochemistry
3
2
1
connective tissue
disorders
(3 weeks)
BCS (1 weeks)
Basic microbiology
& parasitology
(3 weeks)
Basic Infection
& infectious
diseases
(3 weeks)
BCS (1 weeks)
Medical
communication
(3 weeks)
Basic pharmacology
(2 weeks)
BCS (1 weeks)
Studium
Generale
and
Humaniora
(2 weeks)
Basic
Anatomy
( 4 weeks)
& disorders
(3 Weeks)
Metabolism and
Disorders
(4 weeks)
BCS (1 weeks)
Hematologic
system & disorder
& clinical
oncology
(3 weeks)
BCS (1 weeks)
(2 weeks)
Medical
Professionalism
(2 weeks) + medical
ethic (1 weeks)
Basic Anatomy
Pathology & Clinical
pathology (3 weeks)
BCS (1 weeks)
Behavior Change
and disorders
(3 weeks)
Elective Study I
(2 weeks)
The cell
as biochemical
machinery
(2 weeks)
Basic
Histology
(2 weeks) &
Basic
Physiology
(3 weeks)
BCS (1
weeks)
Growth &
developme
nt
(2 weeks)
Basic
Biochemist
ry
(2 weeks)
BCS (1
weeks)
BCS (1 weeks)
Immune system &
disorders
(2 weeks)
BCS (1 weeks)
disorders
(2 weeks)
BCS (1 weeks)
Special Topic
- sexology & anti
aging
- Geriatri
-Travel medicine
(4 weeks)
BCS (1weeks)
Basic
Pharmaceutica
l medicine &
drug etics
19 weeks
(1 weeks)
19 weeks
BCS (1 weeks)
19
weeks
Pendidikan Pancasila & Kewarganegaraan ( 3 weeks )
Inter Professional Education (smt 3-7)
Udayana University Faculty of Medicine, DME, 2015
17