| pubmed-article:6501279 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6501279 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:6501279 | lifeskim:mentions | umls-concept:C0038734 | lld:lifeskim |
| pubmed-article:6501279 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:6501279 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:6501279 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:6501279 | lifeskim:mentions | umls-concept:C1961133 | lld:lifeskim |
| pubmed-article:6501279 | lifeskim:mentions | umls-concept:C2673177 | lld:lifeskim |
| pubmed-article:6501279 | lifeskim:mentions | umls-concept:C0205431 | lld:lifeskim |
| pubmed-article:6501279 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:6501279 | pubmed:dateCreated | 1984-12-27 | lld:pubmed |
| pubmed-article:6501279 | pubmed:abstractText | Three forms of a thiol proteinase inhibitor were isolated from rat liver cytosol. The monomeric inhibitor (pI 5.2) (TPI-1) formed a complex with cathepsin H even in the absence of reducing agents. The inhibitor with pI 5.0 (TPI-2) was inactive in the absence of reducing agents but was converted to an active inhibitor on addition of reducing agents such as dithiothreitol, GSH, cysteine, or 2-mercaptoethanol. The dimeric inhibitor (TPI-D) with an intermolecular disulfide bridge was also inactive and was converted to the active monomeric inhibitor on addition of dithiothreitol. TPI-2 is most likely a mixed disulfide with glutathione. One (Cys-3) of two cysteine residues exposed on the surface of the molecule of TPI-2 is involved in the formation of a mixed disulfide, and the other cysteine residue (Cys-64) is buried in the molecule. The activity of rat liver thiol proteinase inhibitor may possibly be regulated by formation of a protein mixed disulfide or by reduction of the mixed disulfide. | lld:pubmed |
| pubmed-article:6501279 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6501279 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6501279 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6501279 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6501279 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6501279 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6501279 | pubmed:author | pubmed-author:KatunumaNN | lld:pubmed |
| pubmed-article:6501279 | pubmed:author | pubmed-author:KominamiEE | lld:pubmed |
| pubmed-article:6501279 | pubmed:author | pubmed-author:TakioKK | lld:pubmed |
| pubmed-article:6501279 | pubmed:author | pubmed-author:WakamatsuNN | lld:pubmed |
| pubmed-article:6501279 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6501279 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:6501279 | pubmed:volume | 259 | lld:pubmed |
| pubmed-article:6501279 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6501279 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6501279 | pubmed:pagination | 13832-8 | lld:pubmed |
| pubmed-article:6501279 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:6501279 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6501279 | pubmed:articleTitle | Three forms of thiol proteinase inhibitor from rat liver formed depending on the oxidation-reduction state of a sulfhydryl group. | lld:pubmed |
| pubmed-article:6501279 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6501279 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6501279 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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