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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1984-10-3
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pubmed:abstractText |
Properties of cathepsin L from rat liver lysosomes were compared with those of a similar enzyme, cathepsin S from beef spleen. Major characteristics of cathepsin L are the high activity against Z-Phe-Arg-methylcoumarylamide and sensitivity to the fast reacting irreversible inhibitor Z-Phe-Phe-diazomethane. In contrast, cathepsin S hydrolyzes Z-Phe-Arg-methylcoumarylamide only slowly and Z-Phe-Phe-diazomethane cannot be regarded as a potent inhibitor of this enzyme. The differences in the substrate specificity of cathepsin L from rat liver and cathepsin S from beef spleen are discussed in comparison with the substrate specificity of cathepsin B from rat and human liver and beef spleen.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
174
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
123-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6468652-Animals,
pubmed-meshheading:6468652-Cathepsin B,
pubmed-meshheading:6468652-Cathepsin L,
pubmed-meshheading:6468652-Cathepsins,
pubmed-meshheading:6468652-Cattle,
pubmed-meshheading:6468652-Cysteine Endopeptidases,
pubmed-meshheading:6468652-Endopeptidases,
pubmed-meshheading:6468652-Humans,
pubmed-meshheading:6468652-Kinetics,
pubmed-meshheading:6468652-Liver,
pubmed-meshheading:6468652-Lysosomes,
pubmed-meshheading:6468652-Rats,
pubmed-meshheading:6468652-Species Specificity,
pubmed-meshheading:6468652-Spleen,
pubmed-meshheading:6468652-Substrate Specificity
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pubmed:year |
1984
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pubmed:articleTitle |
Species variations amongst lysosomal cysteine proteinases.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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