Effect of alpha 1-proteinase inhibitor and sulphated polysaccharides on the activity of m beta-acrosin.

Abstract:

:Purified m beta-acrosin catalysed amidolysis in vitro of several p-nitroanilides with C-terminal arginine residues. alpha 1-proteinase inhibitor inhibited amidolysis catalysed by the enzyme. This effect of alpha 1-Proteinase inhibitor was not prevented by pre-incubation of the enzyme with heparin or any other glycosaminoglycan. Pre-incubation of the enzyme with sulphated dextran or sulphated cellulose alleviated the effect of alpha 1-proteinase inhibitor. These results are discussed in terms of possible in vivo modulation by alpha 1-proteinase inhibitor of acrosin activity.

authors

Long WF,Williamson FB

doi

10.1016/0006-291x(83)91578-4

subject

Has Abstract

pub_date

1983-11-30 00:00:00

pages

319-23

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)91578-4

journal_volume

117

pub_type

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