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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1976-8-2
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pubmed:abstractText |
The ability of elastatinal and chymostatin, protease inhibitors of microbial origin, to inhibit human leucocyte proteases (EC 3.4.-) was studied. Elastatinal and chymostatin are capable of inhibiting the pancreatic enzymes elastase and chymotrypsin, respectively. It was found in these studies, with synthetic substrates, that elastatinal is a much weaker inhibitor of human leucocyte elastase than it is of porcine pancreatic elastase. Elastatinal caused no inhibition of the activity of human leucocyte chymotrypsin-like protease. Chymostatin was found to be a powerful inhibitor of human leucocyte chymotrypsin-like protease. Its affinity to the leucocyte protease was higher than its affinity to bovine pancreatic alpha-chymotrypsin. Chymsotatin had a weak inhibitory effect on the activity of human leucocyte elastase. Studies were also carried out on the ability of chymostatin to inhibit the release of 35SO2-4 from rabbit articular cartilage by human leucocyte chymotrypsin-like protease. Preincubation of the chymostatin with the protease before the latter was added to the 35SO2-4 -labeled cartilage caused inhibition of proteolysis as measured by 35SO2-4 release. Preincubation of chymostatin with 35SO2-4 -labeled cartilage prior to addition of the human chymotrypsin-like protease to the tissue also inhibited 35SO2-4 release. However, in the case of preincubation of cartilage with alpha1 -antitrypsin there was no such inhibition. It therefore appeared that chymostatin, unlike alpha1 -antitrypsin, was capable of penetrating the cartilage matrix and exerting its inhibitory effect upon the human leucocyte chymotrypsin-like protease that was subsequently added to the tissue.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/alpha 1-Antitrypsin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
429
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
925-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1083745-Animals,
pubmed-meshheading:1083745-Cartilage,
pubmed-meshheading:1083745-Chymotrypsin,
pubmed-meshheading:1083745-Humans,
pubmed-meshheading:1083745-Leukocytes,
pubmed-meshheading:1083745-Oligopeptides,
pubmed-meshheading:1083745-Pancreatic Elastase,
pubmed-meshheading:1083745-Rabbits,
pubmed-meshheading:1083745-Sulfates,
pubmed-meshheading:1083745-alpha 1-Antitrypsin
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pubmed:year |
1976
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pubmed:articleTitle |
The inhibition of human leucocyte elastase and chymotrypsin-like protease by elastatinal and chymostatin.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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