pubmed-article:10990 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10990 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
pubmed-article:10990 | lifeskim:mentions | umls-concept:C0230445 | lld:lifeskim |
pubmed-article:10990 | lifeskim:mentions | umls-concept:C0002003 | lld:lifeskim |
pubmed-article:10990 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:10990 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:10990 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:10990 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:10990 | pubmed:dateCreated | 1977-1-28 | lld:pubmed |
pubmed-article:10990 | pubmed:abstractText | Aldose reductase activity (alditol: NADP+ 1-oxidoreductase, EC 1.1.1.21) from calf brain was separated into two protein fractions by DEAE chromatography. Further purifcation by molecular sieve chromotography and electrofocusing yielding two distinctive enzymes, which were designated AR I and AR II. AR I was purified 646-fold and found to have an isoelectric point of 6.18. AR I was most active as a monomer with a molecular weight of 29 000 and appeared to be in equilibrium with a less active dimer. AR II was purified 425-fold and found to have an isoelectric point of 4.88. The molecular weight of this enzyme was 30 000. Although both enzymes had specificity for aldoses as substrates, AR I had two to three times larger turnover numbers with aromatic aldehydes and hexonates than did AR II. AR I was activated by sulfhydryl compounds and exhibited biphasic double reciprocal plots. AR I was more sensitive to inhibition by high substrate and phenobarbital concentrations than was AR II. AR I and AR II did not have antigenic similarity as tested by Ouchterlony immunodiffusion and counter immunoelectrophoresis. An immunochemical cross-reaction was observed between AR II and lens aldose reductase. | lld:pubmed |
pubmed-article:10990 | pubmed:language | eng | lld:pubmed |
pubmed-article:10990 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10990 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10990 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10990 | pubmed:month | Nov | lld:pubmed |
pubmed-article:10990 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:10990 | pubmed:author | pubmed-author:DoughtyC CCC | lld:pubmed |
pubmed-article:10990 | pubmed:author | pubmed-author:DonsR FRF | lld:pubmed |
pubmed-article:10990 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10990 | pubmed:day | 8 | lld:pubmed |
pubmed-article:10990 | pubmed:volume | 452 | lld:pubmed |
pubmed-article:10990 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10990 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10990 | pubmed:pagination | 1-12 | lld:pubmed |
pubmed-article:10990 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:10990 | pubmed:meshHeading | pubmed-meshheading:10990-Co... | lld:pubmed |
pubmed-article:10990 | pubmed:year | 1976 | lld:pubmed |
pubmed-article:10990 | pubmed:articleTitle | Isolation and characterization of aldose reductase from calf brain. | lld:pubmed |
pubmed-article:10990 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10990 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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