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. 1981 Apr 1;195(1):167-70.
doi: 10.1042/bj1950167.

An inhibitor of collagenase from human amniotic fluid. Purification, characterization and action on metalloproteinases

G Murphy, T E Cawston, J J Reynolds

An inhibitor of collagenase from human amniotic fluid. Purification, characterization and action on metalloproteinases

G Murphy et al. Biochem J. .

Abstract

1. An inhibitor of collagenase of apparent mol.wt. 28000 was isolated from term human amniotic fluid. 2. It is active against mammalian collagenases from a number of species and tissues as well as other mammalian metalloproteinases, but has no activity against bacterial metalloproteinases. 3. Activity is destroyed by treatment with either trypsin or 4-aminophenylmercuric acetate, by heat, and by reduction and carboxymethylation. 4. All the properties observed suggest that it is similar to the synthesized tissue inhibitor of metalloproteinases.

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References

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