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A cryptic protease activity from Trypanosoma cruzi revealed by preincubation with kininogen at low temperatures.

Abstract：

:Cysteine proteases have been identified in parasitic protozoa including the causative agent of Chagas' disease Trypanosoma cruzi. T. cruzi lysates subjected to substrate-containing SDS-polyacrylamide gel electrophoresis exhibit major bands of proteolytic activity in the 45-55 kDa molecular mass range (cruzipain activity). Paradoxically, addition of kininogen (a cystatin-like protease inhibitor) to the lysates before electrophoresis results in the appearance of additional bands of proteolytic activity in the 160-190 kDa molecular mass range. This inhibitor-activated protease activity depends upon the reaction conditions and exhibits novel properties. For example, a 24-48 hour preincubation at low temperature (-20 degrees C optimum) greatly enhances the proteolytic activity. The results suggest that a metastable complex forms between kininogen and a cryptic 30 kDa cysteine protease from T. cruzi and that this complex participates in the activation of proteolytic activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wiser MF,Lonsdale-Eccles JD,D'Alessandro A,Grab DJ

doi

10.1006/bbrc.1997.7690

subject

Has Abstract

pub_date

1997-11-26 00:00:00

pages

540-4

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)97690-7

journal_volume

240

pub_type

杂志文章

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