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

G Murphy; P Koklitis; A F Carne

doi:10.1042/bj2611031

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

Biochem J. 1989 Aug 1;261(3):1031-4. doi: 10.1042/bj2611031.

Authors

G Murphy¹, P Koklitis, A F Carne

Affiliation

¹ Strangeways Research Laboratory, Cambridge, 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Chromatography, Gel
Enzyme Inhibitors / metabolism*
Humans
Matrix Metalloproteinase 3
Metalloendopeptidases / antagonists & inhibitors*
Molecular Sequence Data
Tissue Inhibitor of Metalloproteinases

Substances

Enzyme Inhibitors
Tissue Inhibitor of Metalloproteinases
Metalloendopeptidases
Matrix Metalloproteinase 3