Lancaster EPrints

Preliminary characterisation of esterase and platelet-activating factor (PAF)-acetylhydrolase activities from cat flea (Ctenocephalides felis) salivary glands

Cheeseman, M T and Bates, P A and Crampton, J M (2001) Preliminary characterisation of esterase and platelet-activating factor (PAF)-acetylhydrolase activities from cat flea (Ctenocephalides felis) salivary glands. Insect biochemistry and molecular biology, 31 (2). pp. 157-164. ISSN 0965-1748

Full text not available from this repository.

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 alpha-naphthyl acetate (approximately 210pmol/min/gland pair; 10.0micromol/min/mg specific activity; K(m) approximately 59microM) and beta-naphthyl acetate (approximately 110pmol/min/gland pair; 5.2micromol/min/mg specific activity; K(m) approximately 132microM). Salivary gland extracts have PAF-acetylhydrolase activity (approximately 5pmol/min/gland pair; 0.24micromol/min/mg specific 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 approximately 56kDa, approximately 57kDa and approximately 58kDa 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 approximately 59kDa. This partially purified pool of enzyme had esterase activity against a series of short-chain alpha- and beta-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.

Item Type: Article
Journal or Publication Title: Insect biochemistry and molecular biology
Uncontrolled Keywords: Cat flea (Ctenocephalides felis) ; Salivary gland ; Saliva ; Esterase ; Glycoprotein ; Platelet-activating factor (PAF) ; PAF-acetylhydrolase
Subjects: Q Science > QR Microbiology > QR355 Virology
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 56296
Deposited By: ep_importer_pure
Deposited On: 27 Jul 2012 15:10
Refereed?: Yes
Published?: Published
Last Modified: 27 Jul 2012 15:10
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/56296

Actions (login required)

View Item