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Proteolytic activity in Tritrichomonas mobilensis

Published online by Cambridge University Press:  06 April 2009

P. Bózner ,
P. Demeš  and
J. Štefanovič
P. Bózner
Affiliation:
Department of Microbiology and Immunology and Czechoslovakia
P. Demeš
Affiliation:
Institute of Immunology, Comenius University, Sasinkova 4, 811 08 Bratislava, Czechoslovakia
J. Štefanovič
Affiliation:
Department of Microbiology and Immunology and Czechoslovakia
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Summary

Cell extracts of an entero-invasive protozoon of squirrel monkeys, Tritrichomonas mobilensis, contained relatively high proteolytic activity, measured on hide powder azure (HPA). Multiple proteinase forms, optimally active at pH 5–7, were detected by electrophoretic analysis in gelatin-containing polyacrylamide gels. Three major proteinase bands of apparent low molecular weights, Mr 18, 23 and 30 kDa, were seen on gels. Inhibition-activation studies suggest that only cysteine proteinases were involved in HPAase and gelatinolytic activities of T. mobilensis cell extracts.

Keywords

Tritrichomonas mobilensistrichomonad proteinasescysteine proteinases
Type
Research Article
Information
Parasitology , Volume 101 , Issue 1 , August 1990 , pp. 57 - 60
Copyright
Copyright © Cambridge University Press 1990

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