| pubmed-article:2044774 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2044774 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:2044774 | lifeskim:mentions | umls-concept:C0054871 | lld:lifeskim |
| pubmed-article:2044774 | lifeskim:mentions | umls-concept:C0054874 | lld:lifeskim |
| pubmed-article:2044774 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:2044774 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:2044774 | lifeskim:mentions | umls-concept:C0728938 | lld:lifeskim |
| pubmed-article:2044774 | lifeskim:mentions | umls-concept:C0205197 | lld:lifeskim |
| pubmed-article:2044774 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2044774 | pubmed:dateCreated | 1991-7-17 | lld:pubmed |
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| pubmed-article:2044774 | pubmed:abstractText | The complete amino acid sequence of bovine spleen cathepsin S has been determined. The single-chain protein contains 217 residues and has a Mr of 23,682. The primary structure was determined by sequencing of native protein and the peptides obtained by proteolytic cleavage with beta-trypsin, papaya proteinase IV and by chemical cleavage with cyanogen bromide. Comparison of the amino terminal sequences of the heavy and the light chain of bovine cathepsin L with that of bovine cathepsin S clearly indicates that the enzymes are structurally different. | lld:pubmed |
| pubmed-article:2044774 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2044774 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2044774 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2044774 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2044774 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2044774 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2044774 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2044774 | pubmed:author | pubmed-author:TurkVV | lld:pubmed |
| pubmed-article:2044774 | pubmed:author | pubmed-author:DolencII | lld:pubmed |
| pubmed-article:2044774 | pubmed:author | pubmed-author:RitonjaAA | lld:pubmed |
| pubmed-article:2044774 | pubmed:author | pubmed-author:PodobnikMM | lld:pubmed |
| pubmed-article:2044774 | pubmed:author | pubmed-author:Coli?AA | lld:pubmed |
| pubmed-article:2044774 | pubmed:author | pubmed-author:OgrincTT | lld:pubmed |
| pubmed-article:2044774 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2044774 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:2044774 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:2044774 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2044774 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2044774 | pubmed:pagination | 329-31 | lld:pubmed |
| pubmed-article:2044774 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2044774 | pubmed:meshHeading | pubmed-meshheading:2044774-... | lld:pubmed |
| pubmed-article:2044774 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2044774 | pubmed:articleTitle | The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L. | lld:pubmed |
| pubmed-article:2044774 | pubmed:affiliation | Department of Biochemistry, Jozef Stefan Institute, Ljubljana, Yugoslavia. | lld:pubmed |
| pubmed-article:2044774 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2044774 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2044774 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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