title: 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).
authors.affiliation: Departamento de Bioquímica, Instituto Nacional de Perinatología, SS, México, D.F.
authors.forename: F
authors.initials: F
authors.lastname: Vadillo-Ortega
authors.forename: G
authors.initials: G
authors.lastname: González-Avila
authors.forename: I
authors.initials: I
authors.lastname: Montfort
authors.forename: L
authors.initials: L
authors.lastname: Bermejo
authors.forename: R
authors.initials: R
authors.lastname: Pérez-Tamayo
mesh_terms: D000818:Animals; D002853:Chromatography, Liquid; D017364:Collagenases / Q000737:chemistry / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D007668:Kidney / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D051381:Rats; D017208:Rats, Wistar
chemical_list: D017364:Collagenases