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Titolo:
Preliminary characterisation of esterase and platelet-activating factor (PAF)-acetylhydrolase activities from cat flea (Ctenocephalides felis) salivary glands
Autore:
Cheeseman, MT; Bates, PA; Crampton, JM;
Indirizzi:
Univ Liverpool, Dept Vet Pathol, Liverpool L69 3BX, Merseyside, England Univ Liverpool Liverpool Merseyside England L69 3BX , Merseyside, England Univ Liverpool, Liverpool Sch Trop Med, Liverpool L3 5QA, Merseyside, England Univ Liverpool Liverpool Merseyside England L3 5QA A, Merseyside, England Univ Liverpool, Sch Biol Sci, Liverpool L3 5QA, Merseyside, England Univ Liverpool Liverpool Merseyside England L3 5QA A, Merseyside, England
Titolo Testata:
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
fascicolo: 2, volume: 31, anno: 2001,
pagine: 157 - 164
SICI:
0965-1748(200102)31:2<157:PCOEAP>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
LONE STAR TICK; SWEET ITCH; EOSINOPHILS; ARTHROPODS; APYRASE; HORSES;
Keywords:
cat flea (Ctenocephalides felis); salivary gland; saliva; esterase; glycoprotein; platelet-activating factor (PAF); PAF-acetylhydrolase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Cheeseman, MT Univ London Royal Vet Coll, Dept Pathol & Infect Dis, Hawkshead Lane, Hatfield AL9 7TA, Herts, England Univ London Royal Vet Coll Hawkshead Lane Hatfield Herts England AL9 7TA
Citazione:
M.T. Cheeseman et al., "Preliminary characterisation of esterase and platelet-activating factor (PAF)-acetylhydrolase activities from cat flea (Ctenocephalides felis) salivary glands", INSEC BIO M, 31(2), 2001, pp. 157-164

Abstract

Naphthyl esterase and platelet-activating factor (PAF)-acetylhydrolase activities were detected in the salivary glands of the cat flea, Ctenocephnlides felis. Salivary naphthyl esterase activity is disgorged during exploratory probing. Whole extracts of salivary glands contain esterase activity against the short-chain naphthyl esters a-naphthyl acetate (similar to 210 pmol/min/gland pair; 10.0 mu mol/min/mg specific activity; K(m)similar to 59 muM) and beta -naphthyl acetate (similar to 110 pmol/min/gland pair; 5.2 mu mol/min/mg specific activity; K(m)similar to 132 muM). Salivary gland extracts have PAF-acetylhydrolase activity (similar to5 pmol/min/gland pair; 0.24 mu mol/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 fromcarcass 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 similar to 56 kDa, similar to 57 kDa and similar to 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 similar to 59 kDa. 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. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 07:42:31