Plasmin converts pro-form of group I phospholipase A2 into receptor binding, active forms.
作者信息
Nakano T, Fujita H, Kikuchi N, Arita H
机构信息
Shionogi Research Laboratories, Shionogi & Co. Ltd., Osaka, Japan.
出版信息
Biochem Biophys Res Commun. 1994 Jan 14;198(1):10-5. doi: 10.1006/bbrc.1994.1002.
PMID:8292010
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.
摘要
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