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PMID: 6307277 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The interaction of purified rabbit bone collagenase with purified rabbit bone metalloproteinase inhibitor.

The Biochemical journal ·Vol. 211 ·No. 2 ·1983-05-01 ·Pages 313-8

Cawston TE, Murphy G, Mercer E, Galloway WA, Hazleman BL, Reynolds JJ

Abstract

1. Pure rabbit bone metalloproteinase inhibitor (TIMP) bound tightly to pure rabbit bone collagenase with an apparent Kd of 1.4 X 10(-10) M. 2. The molecular weight of the enzyme-inhibitor complex was found to be 54 000, but no enzyme activity could be recovered from the complex after treatment with either mercurials or proteinases. The complex thus differed from latent collagenase in terms of size, susceptibility to mercurials and behaviour on concanavalin A-Sepharose. 3. The interaction of the purified components was compared with that of crude collagenase and crude inhibitor in culture medium. Mercurial treatment partially reversed the inhibition in the crude system, but not when the purified components were used. 4. The significance of the results is discussed in relation to the extracellular control of the activity of collagenase.

MeSH Terms
Animals Bone and Bones/enzymology Chromatography, Gel Enzyme Inhibitors/metabolism Kinetics Macromolecular Substances Mercury/pharmacology Microbial Collagenase/antagonists & inhibitors,metabolism Molecular Weight Rabbits Sepharose/analogs & derivatives,metabolism Tissue Inhibitor of Metalloproteinases
Chemicals
Enzyme Inhibitors Macromolecular Substances Tissue Inhibitor of Metalloproteinases concanavalin A-sepharose Sepharose Microbial Collagenase Mercury
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Cawston T E
Murphy G
Mercer E
Galloway W A
Hazleman B L
Reynolds J J
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22 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1983-05-01
Pages
313-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1154361
Subset
IM
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