pubmed-article:2644137 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
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pubmed-article:2644137 | lifeskim:mentions | umls-concept:C0021641 | lld:lifeskim |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C0037657 | lld:lifeskim |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C1441672 | lld:lifeskim |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:2644137 | lifeskim:mentions | umls-concept:C0063651 | lld:lifeskim |
pubmed-article:2644137 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2644137 | pubmed:dateCreated | 1989-3-23 | lld:pubmed |
pubmed-article:2644137 | pubmed:abstractText | An insulin-degrading enzyme has been purified from human erythrocytes. This enzyme degraded 125I-labeled insulin-like growth factor I (IGF-I) more slowly than 125I-IGF-II and degraded IGF-II more slowly than 125I-insulin. The time course of 125I-insulin degradation suggested the presence of intermediates, each of which was itself shown to be a substrate for the enzyme. One of these intermediates appeared to be made up entirely of B-chain residues and had HisB10 as its NH2-terminal. The final major radiolabeled degradation product of A14-[125I]monoiodoinsulin was a peptide with TyrA14 at the A-chain NH2 terminal. This peptide could be reduced with dithiothreitol, suggesting that it contained amino acid residues from both A- and B-chains. It was partially precipitated by trichloroacetic acid and anti-insulin antibody but bound poorly to IM-9 lymphocytes. The final major degradation product of B26-[125I]monoiodoinsulin was a peptide whose NH2-terminal was TyrB26 and could not be reduced by dithiothreitol. It was partially precipitated by anti-insulin antibody but was precipitated poorly, if at all, by trichloroacetic acid and bound poorly to IM-9 lymphocytes. The results show that this enzyme degraded insulin by sequential cleavage of peptide bonds on both A- and B-chains. We identified LeuA13-TyrA14, SerB9-HisB10, and PheB25-TyrB26 as three of the bonds that are cleaved. | lld:pubmed |
pubmed-article:2644137 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2644137 | pubmed:language | eng | lld:pubmed |
pubmed-article:2644137 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2644137 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:2644137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2644137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2644137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2644137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2644137 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2644137 | pubmed:month | Feb | lld:pubmed |
pubmed-article:2644137 | pubmed:issn | 0012-1797 | lld:pubmed |
pubmed-article:2644137 | pubmed:author | pubmed-author:MisbinR IRI | lld:pubmed |
pubmed-article:2644137 | pubmed:author | pubmed-author:AlmiraE CEC | lld:pubmed |
pubmed-article:2644137 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2644137 | pubmed:volume | 38 | lld:pubmed |
pubmed-article:2644137 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2644137 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2644137 | pubmed:pagination | 152-8 | lld:pubmed |
pubmed-article:2644137 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:2644137 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2644137 | pubmed:articleTitle | Degradation of insulin and insulin-like growth factors by enzyme purified from human erythrocytes. Comparison of degradation products observed with A14- and B26-[125I]monoiodoinsulin. | lld:pubmed |
pubmed-article:2644137 | pubmed:affiliation | Division of Endocrinology and Metabolism, University of Florida College of Medicine, Gainesville 32610. | lld:pubmed |
pubmed-article:2644137 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2644137 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2644137 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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