Proteolytic activity inTritrichomonas mobilensis

Abstract

SUMMARYCell 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,Mr18, 23 and 30 kDa, were seen on gels. Inhibition-activation studies suggest that only cysteine proteinases were involved in HPAase and gelatinolytic activities ofT. mobilensiscell extracts.