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Proteolytic activity in Tritrichomonas mobilensis

Published online by Cambridge University Press:  06 April 2009

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

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.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1990

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