Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Collagenase of human basal cell epithelioma was purified by sequential ammonium sulfate precipitation, Sephadex gel filtration and affinity chromatography on collagen-polyacrylamide gel. The collagenase, when partially purified, was found to have an approximate molecular weight of 50,000. The purified enzyme contained no caseinolytic activity. On polyacrylamide gel electrophoresis, the purified enzyme gave a single protein band. The purified collagenase cleaved native acid-soluble guinea pig skin collagen at 37 degrees C with a pH optimum of 8. The enzyme was inhibited by EDTA, cysteine, and human serum but not by soybean trypsin inhibitor. Heparin did not stimulate the enzyme activity. Purified collagenase reduced the specific viscosity of native acid-soluble guinea pig skin collagen to 50 per cent of its original value at 27 degrees C. Polyacrylamide gel disc electrophoresis of the reaction products showed bands corresponding to alphaA, betaA, and alphaB fragments. Electron microscopic examination of SLS aggregates of the reaction products showed that the cleavage site by the enzyme was at a point 75 per cent from the "A" end (TCA75) and 25 per cent from the "B" end (TCB25) of the collagen molecule.
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PMID:Collagenase of human skin basal cell epithelioma. 1 52

Digestion of the cuticle collagen from the annelid Nereis virens with Clostridium histolyticum collagenase yields a native, collagenase-resistant fragment (CCRF) of the molecule with an Mr of about 900,000 (Kimura and Tanzer, J. Biol. Chem. 252: 8018, 1977). We have produced 940 nm long, SLS-crystallites from the collagenase-resistant fragment; the SLS pattern matches a region at one end of the 2,400 nm SLS obtained from intact cuticle collagen. Upon denaturation, the fragment yields two subunits, CCRFA and CCRFB, which can be separated by SDS polyacrylamide gel electrophoresis or by chromatography on DEAE-cellulose; the subunits are in about a 2:1 ratio. The subunits have amino acid compositions which are similar to those of the original A and B chains, although the fragments have a higher content of acidic residues and a lower content of hydroxyl residues. Previous studies of the intact B chain have shown that there is about one methionine in the chain, and that it is located near the COOH terminus. The CCRFB subunit also contains about one methionine, indicating that CCRFB is probably derived from the COOH end of the intact molecule. Based on these composite data, we have provisionally defined the amino and carboxyl ends of the cuticle collagen SLS and provide additional evidence that the molecule is a heteropolymer with the formula A(B)2.
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PMID:Characterization of a large fragment from annelid cuticle collagen and its relationship to the intact molecule. 632 Oct 95