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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
1984-12-27
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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.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin H,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsh protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13832-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6501279-Amino Acids,
pubmed-meshheading:6501279-Animals,
pubmed-meshheading:6501279-Cathepsin H,
pubmed-meshheading:6501279-Cathepsins,
pubmed-meshheading:6501279-Chromatography, DEAE-Cellulose,
pubmed-meshheading:6501279-Chromatography, Gel,
pubmed-meshheading:6501279-Cysteine,
pubmed-meshheading:6501279-Cysteine Endopeptidases,
pubmed-meshheading:6501279-Glutathione,
pubmed-meshheading:6501279-Isoenzymes,
pubmed-meshheading:6501279-Liver,
pubmed-meshheading:6501279-Male,
pubmed-meshheading:6501279-Molecular Weight,
pubmed-meshheading:6501279-Oxidation-Reduction,
pubmed-meshheading:6501279-Protease Inhibitors,
pubmed-meshheading:6501279-Protein Conformation,
pubmed-meshheading:6501279-Rats,
pubmed-meshheading:6501279-Rats, Inbred Strains,
pubmed-meshheading:6501279-Sulfhydryl Compounds
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pubmed:year |
1984
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pubmed:articleTitle |
Three forms of thiol proteinase inhibitor from rat liver formed depending on the oxidation-reduction state of a sulfhydryl group.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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