Introduction Directory UMM :Data Elmu:jurnal:I:Insect Biochemistry and Molecular Biology:Vol31.Issue2.Feb2001:
Insect Biochemistry and Molecular Biology 31 2001 157–164 www.elsevier.comlocateibmb
Preliminary characterisation of esterase and platelet-activating factor PAF-acetylhydrolase activities from cat flea
Ctenocephalides felis salivary glands
M.T. Cheeseman
a,
, P.A. Bates
b
, J.M. Crampton
c
a
Department of Veterinary Pathology, University of Liverpool, Liverpool, UK
b
Liverpool School of Tropical Medicine, University of Liverpool, Liverpool, UK
c
School of Biological Sciences, University of Liverpool, Liverpool, UK Received 19 January 2000; received in revised form 1 June 2000; accepted 6 June 2000
Abstract
Naphthyl esterase and platelet-activating factor PAF-acetylhydrolase activities were detected in the salivary glands of the cat flea, Ctenocephalides felis. Salivary naphthyl esterase activity is disgorged during exploratory probing. Whole extracts of salivary
glands contain esterase activity against the short-chain naphthyl esters α
-naphthyl acetate |210 pmolmingland pair; 10.0
µ molminmg specific activity; K
m
|59 µ
M and β
-naphthyl acetate |110 pmolmingland pair; 5.2 µ
molminmg specific activity; K
m
|132 µ
M. Salivary gland extracts have PAF-acetylhydrolase activity |5 pmolmingland pair; 0.24 µ
molminmg spe- cific activity but do not have detectable acetylcholinesterase activity. Native–PAGE and IEF resolve three and six salivary gland
naphthyl esterase bands, respectively, and both patterns are different from carcass esterases. Salivary gland naphthyl esterase activity binds reversibly to Concanavalin A, and enzymatic deglycosylation with glycopeptidase F produced a new, fast-migrating salivary
gland naphthyl esterase band on Native–PAGE. Renaturation of esterase activity after SDS–PAGE gave |56 kDa, |57 kDa and |58 kDa naphthyl-esterase-positive bands. On gel filtration naphthyl esterase and PAF-acetylhydrolase activities co-elute as a single
peak with an apparent molecular weight of |59 kDa. This partially purified pool of enzyme had esterase activity against a series of short-chain
α - and
β -naphthyl esters. The heterogeneity of salivary gland esterases, their relationship to PAF-acetylhydrolase,
and the possible physiological functions of salivary gland PAF-acetylhydrolase activity are discussed.
2001 Elsevier Science Ltd. All rights reserved.
Keywords: Cat flea Ctenocephalides felis; Salivary gland; Saliva; Esterase; Glycoprotein; Platelet-activating factor PAF; PAF-acetylhydrolase