| pubmed-article:6468652 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6468652 | lifeskim:mentions | umls-concept:C2717970 | lld:lifeskim |
| pubmed-article:6468652 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:6468652 | lifeskim:mentions | umls-concept:C1705920 | lld:lifeskim |
| pubmed-article:6468652 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6468652 | pubmed:dateCreated | 1984-10-3 | lld:pubmed |
| pubmed-article:6468652 | 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. | lld:pubmed |
| pubmed-article:6468652 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6468652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6468652 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6468652 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6468652 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:6468652 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:6468652 | pubmed:author | pubmed-author:KirschkeHH | lld:pubmed |
| pubmed-article:6468652 | pubmed:author | pubmed-author:TurkVV | lld:pubmed |
| pubmed-article:6468652 | pubmed:author | pubmed-author:LocnikarPP | lld:pubmed |
| pubmed-article:6468652 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6468652 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:6468652 | pubmed:volume | 174 | lld:pubmed |
| pubmed-article:6468652 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6468652 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6468652 | pubmed:pagination | 123-7 | lld:pubmed |
| pubmed-article:6468652 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:6468652 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6468652 | pubmed:articleTitle | Species variations amongst lysosomal cysteine proteinases. | lld:pubmed |
| pubmed-article:6468652 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6468652 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:6468652 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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