Properties of the acid thiol proteinase from Schistosoma mansoni adults.

Abstract:

:Seven beta-naphthylamine-linked peptides were tested as substrates for a previously described thiol proteinase of adult Schistosoma mansoni. The enzyme was not active on carbobenoxy-arginyl-arginyl-4-methoxy-2-naphthylamide and carbobenzoxy-alanyl-arginyl-arginyl-4-methoxy-2-naphthylamide. Enzyme activity was maximal at acidic pH (4.9-5.5) with similar optima for both macromolecular and peptide substrates. Activity of partially purified enzyme preparations against carbobenzoxy-arginyl-arginyl-4-methoxy-2-naphthylamide was stimulated more than 10-fold by thiols. The properties of this proteinase differ from those of proteolytic enzymes from the cercariae ad eggs of S. mansoni.

journal_name

Mol Biochem Parasitol

authors

Dresden MH,Rutledge ML,Chappell CL

doi

10.1016/0166-6851(81)90029-3

subject

Has Abstract

pub_date

1981-11-01 00:00:00

pages

61-6

issue

1-2

eissn

0166-6851

issn

1872-9428

pii

0166-6851(81)90029-3

journal_volume

4

pub_type

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