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Characterization of peptidases of adult Trichuris muris

Published online by Cambridge University Press:  06 April 2009

L. J. Drake ,
A. E. Bianco ,
D. A. P. Bundy  and
F. Ashall
L. J. Drake
Affiliation:
Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, South Kensington, London SW7 2BB
A. E. Bianco
Affiliation:
Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, South Kensington, London SW7 2BB
D. A. P. Bundy
Affiliation:
Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, South Kensington, London SW7 2BB
F. Ashall
Affiliation:
Department of Biology, Imperial College of Science, Technology and Medicine, Prince Consort Road, South Kensington, London SW7 2BB
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Extract

Excretory/secretory (E/S) material of Trichuris muris was found to contain 2 major peptidases, Mr 85 and 105 kDa, which degrade gelatin optimally at pH 6·0 in sodium dodecyl sulphate–polyacrylamide gels. The peptidases were inactivated diisopropylfluorophosphate, leupeptin and soybean trypsin inhibitor, but were unaffected by inhibitors of aspartic-, cysteine- and metallo-peptidases, indicating that they are serine peptidases. Both enzymes were detectable within 5 h after incubation of worms in culture medium and showed a time-dependent increase in levels. Neither peptidase was detected in worm extracts, suggesting that they are activated during or following secretion from worms. Live worms degraded radio-isotope labelled extracellular matrix protein substratum derived from mammalian cells. Aminopeptidase activities capable of catalysing hydrolysis of amino acyl aminomethylcoumarin (MCA) substrates and a Z-Phe-Arg-MCA-hydrolysing cysteine peptidase activity, were detected in extracts of adult worms but not in E/S material.

Keywords

peptidaseTrichuris murisexcretory/secretory materialserine peptidase
Type
Research Article
Information
Parasitology , Volume 109 , Issue 5 , December 1994 , pp. 623 - 630
Copyright
Copyright © Cambridge University Press 1994

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