title: High molecular mass type i.v. collagen-specific metalloprotease from human carcinoma tissue.
abstract: A protease degrading type IV collagen was purified more than 8000-fold from human stomach carcinoma tissue. This protease degraded type IV collagen, while type I, II, III and V collagen, laminin, fibronectin, casein, albumin and hemoglobin were not affected. This enzyme had a pH optimum of pH 7.0-8.0 and was inhibited completely by EDTA and o-phenanthroline, but not by seryl, thiol and carboxyl protease inhibitors. Furthermore, the molecular mass of this enzyme was estimated to be 1 MDa by Sepharose 6B column and HPLC-gel filtration. The molecular mass and substrate specificity of this metalloprotease from human carcinoma tissue indicate it to be a new protease.
authors: Department of Biochemistry, School of Medicine, Tokai University, Kanagawa, Japan.
authors: M
authors: M
authors: Tsuda
authors: Y
authors: Y
authors: Yamagishi
authors: T
authors: T
authors: Katsunuma
mesh_terms: D002845:Chromatography; D002851:Chromatography, High Pressure Liquid; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D013274:Stomach Neoplasms / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D003094:Collagen; D008666:Metalloendopeptidases