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Inhibition of activated protein C by aprotinin and the use of the insolubilized inhibitor for its purification.

Abstract：

:The study of the interaction between activated protein C (APC) and non-plasmatic inhibitors allowed us to demonstrate that aprotinin is a potent competitive inhibitor of APC with a Ki of 1.35 mumol/L. It was possible to adsorb immunopurified protein C (PC) activated by venom activator to insolubilized aprotinin and to recover the active enzyme after elution by HCl 0.1 N or by a chaotropic ion, for example KSCN 3 mol/L. The interaction involved the active-site of the enzyme since PC and DIP-APC did not bind to the matrix. Thus, APC could be purified, after activation, in a one-stage procedure out of a mixture of protein such as a prothrombin complex concentrate.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Taby O,Chabbat J,Steinbuch M

doi

10.1016/0049-3848(90)90268-h

subject

Has Abstract

pub_date

1990-07-01 00:00:00

pages

27-35

issue

1

eissn

0049-3848

issn

1879-2472

journal_volume

59

pub_type

杂志文章

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