Dissociation of tissue inhibitor of metalloproteinases (TIMP) from enzyme complexes yields fully active inhibitor-Reference-Cited by-同舟云学术

Dissociation of tissue inhibitor of metalloproteinases (TIMP) from enzyme complexes yields fully active inhibitor

Published:1989-08-01 Issue:3 Volume:261 Page:1031-1034
ISSN:0264-6021
Container-title:Biochemical Journal
language:en
Short-container-title:

Author:

Murphy G¹,Koklitis P²,Carne A F²

Affiliation:

1. Strangeways Research Laboratory, Cambridge CBI 4RN.

2. Celltech Ltd., 216 Bath Road, Slough SLI 4EN, Berks., U.K.

Abstract

Recombinant human tissue inhibitor of metalloproteinases (TIMP) forms complexes with high-Mr active recombinant stromelysin that are stable over long periods under physiological conditions. TIMP-stromelysin complexes could be dissociated in the presence of EDTA at pH 3, releasing free TIMP and destroying stromelysin activity. The dissociated TIMP was apparently unmodified, in contrast with other known protein inhibitors of metalloproteinases and many classes of serine-proteinase inhibitor, which are slowly cleaved.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://portlandpress.com/biochemj/article-pdf/261/3/1031/597424/bj2611031.pdf

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