PURIFICATION AND PARTIAL CHARACTERIZATION OF A CYSTEINE PROTEINASE FROM TRYPANOSOMA-RANGELI

被引：9

作者：

LABRIOLA, C

CAZZULO, JJ

机构：

[1] nstituto de Investigaciones Bioquímicas, Fundación Campomar A. Machado 151

来源：

FEMS MICROBIOLOGY LETTERS | 1995年 / 129卷 / 2-3期

关键词：

TRYPANOSOMA RANGELI; CYSTEINE PROTEINASE; CRUZIPAIN;

D O I：

10.1016/0378-1097(95)00148-X

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Epimastigotes of the American Trypanosome Trypanosoma rangeli contain a very low cysteine proteinase (CP) activity. The enzyme was purified to homogeneity by affinity chromatography on ConA-Sepharose and Cystatin-Sepharose. This CP had a similar apparent molecular mass and an identical N-terminal sequence (15 amino acids) as compared with cruzipain from Trypanosoma cruzi; cross-reacted immunologically with the latter enzyme, it was inhibited by E-64 and TLCK, but not by PMSF, o-phenanthroline or Pepstatin, and was able to use the same substrates, although with different order of effectiveness and optimum pH.

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页码：143 / 148

页数：6

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