Plasmin converts pro-form of group I phospholipase A2 into receptor binding, active forms.

Abstract:

:Treatment of zymogen of pancreatic-type group I phospholipase A2 (PLA2-I) by plasmin, a fibrinolytic enzyme, increases PLA2 activity as well as receptor binding activity in a dose- and time-dependent manner. Separation of plasmin-treated pro-PLA2-I by HPLC and amino acid sequence analysis of the products revealed that, in addition to an authentic mature PLA2-I produced by trypsin, plasmin produced active products which had been modified in the C-terminal region. Thus, PLA2-I may be involved in physiologic processes which accompany the formation of plasmin.

authors

Nakano T,Fujita H,Kikuchi N,Arita H

doi

10.1006/bbrc.1994.1002

subject

Has Abstract

pub_date

1994-01-14 00:00:00

pages

10-5

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)71002-3

journal_volume

198

pub_type

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