Proteolytic activity in Tritrichomonas mobilensis.
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.
Bózner
P
P
Department of Microbiology and Immunology, Comenius University, Bratislava, Czechoslovakia.
Demes
P
P
Stefanovic
J
J
D000818:Animals; D003124:Colorimetry; D003546:Cysteine Endopeptidases / Q000032:analysis / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis* / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D012453:Saimiri; D014318:Tritrichomonas / Q000201:enzymology*
D010450:Endopeptidases; D003546:Cysteine Endopeptidases