Extraction and partial characterization of a low molecular weight collagenase from normal rat kidney.

Abstract:

:A matrix metalloproteinase with selective affinity for collagen was identified and partially purified from normal rat kidney. A two-step purification procedure consisting of gel filtration and affinity chromatography on Sepharose 4B-collagen resulted in an increase in specific activity of more than 3,000 times. The partially purified collagenase cleaved type I collagen and also showed low gelatinolytic activity. The enzyme required Ca2+ and revealed a neutral pH optimum; it was not inhibited by thiol or serineprotease inhibitors. Its activity was fully blocked using recombinant tissue inhibitor of metalloproteinases-1. Using SDS-PAGE and zymography, the estimated Mr of the collagenase was 16.5 x 10(3).

journal_name

Arch Med Res

authors

Vadillo-Ortega F,González-Avila G,Montfort I,Bermejo L,Pérez-Tamayo R

subject

Has Abstract

pub_date

1995-10-01 00:00:00

pages

273-8

issue

3

eissn

0188-4409

issn

1873-5487

journal_volume

26

pub_type

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