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)

The substrate specificity of two isozymes of collagenolytic protease of the crab (Paralithodes camtschatica) was studied. It was found that both proteases can effectively hydrolyze type I and III collagens, as well as gelatin, the set of products yielded by enzymatic hydrolysis being different for isozymes A and C. Hydrolysis of some well-known peptides revealed that isozyme A predominantly cleaves the peptide bonds containing arginine and lysine residues, whereas isozyme C predominantly hydrolyzes bonds containing hydrophobic amino acids. The catalytic constants for the hydrolysis of several low molecular weight substrates in the presence of P. camtschatica proteases were determined, which allowed to attribute isozyme A to trypsin-like, and isozyme C to chymotrypsin-like proteinases. The peptide substrates of collagenase, Pz-Pro-Leu-Gly-Pro-D-Arg and Z-Gly-Pro-Ala-Gly-Pro-Ala are not hydrolyzed isozymes of crab collagenolytic protease.
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PMID:[Substrate specificity of collagenolytic proteases from the hepatopancreas of the of the Kamchatka crab]. 139 Dec 5

We compared the in vitro degradation of porcine and human insulin in the subcutaneous tissue of rat. The insulin degrading activity was largely confined to the 160000 X g supernatant fraction of subcutaneous tissue. The degradation of human insulin was approximately half that of porcine insulin in the supernatant fraction. The degradation of porcine insulin in subcutaneous tissue was inhibited by bacitracin, leupeptin, phosphoramidon, and Z-Gly-Pro-Leu-Gly, though the human insulin degradation was not. The degradation of both insulins was accelerated by glutathione. While the proteolytic enzyme activities of cathepsin-B and collagenase-like peptidase were detectable in subcutaneous tissue, chymotrypsin, elastase, kallikrein, alpha-thrombin, and trypsin activities were almost negligible. These in vitro studies suggest that human insulin is comparatively stable against proteolytic enzymes, probably collagenase-like peptidase or cathepsin-B, in the subcutaneous tissue, which support the in vivo evidence.
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PMID:Fate of porcine and human insulin at the subcutaneous injection site. II. In vitro degradation of insulins in the subcutaneous tissue of the rat. 240 62