Cysteine proteinase of Entamoeba histolytica. I. Partial purification and action on different enzymes.

Abstract:

:A method for a 50-60-fold purification of a cysteine proteinase from trophozoites of Entamoeba histolytica using 35-80% ammonium sulphate fractionation, gel chromatography on Sephadex G-75, and preparative isoelectric focusing is described. The enzyme was examined for its proteolytic potencies towards native enzyme substrates. The amebic proteinase directly inactivates aldolase and glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle as well as glucose-6-phosphate dehydrogenase from yeast. The inactivation of citrate synthase from porcine heart proceeds rather slowly, whereas malate dehydrogenase from porcine heart is not affected by the amebic proteinase under the condition used. With the exception of aldolase all inactivated enzyme substrates have been cleaved by limited proteolyses yielding major cleavage products. The inactivation of aldolase probably functions by the release of a small segment from a terminus being essential for aldolase activity.

journal_name

Mol Biochem Parasitol

authors

Scholze H,Werries E

doi

10.1016/0166-6851(86)90054-x

subject

Has Abstract

pub_date

1986-01-01 00:00:00

pages

103-12

issue

1

eissn

0166-6851

issn

1872-9428

pii

0166-6851(86)90054-X

journal_volume

18

pub_type

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