| pubmed-article:6151948 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C1267092 | lld:lifeskim |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C0003483 | lld:lifeskim |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C2263085 | lld:lifeskim |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C0001477 | lld:lifeskim |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:6151948 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:6151948 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:6151948 | pubmed:dateCreated | 1985-3-27 | lld:pubmed |
| pubmed-article:6151948 | pubmed:abstractText | An acid-stable phosphoprotein was formed in a microsomal membrane fraction isolated from bovine aortic smooth muscle in the presence of Mg2+ + ATP and Ca2+. The microsomes also showed Ca2+ uptake activity. The Ca2+ dependence of phosphoprotein formation and of Ca2+ uptake occurred over the same range of Ca2+ concentration (1-10 microM), and resembled similar findings from rabbit skeletal microsomes. The molecular weight of the phosphorylated protein, estimated by SDS-gel electrophoresis, was approximately 105,000. The phosphoprotein was labile at alkaline pH, and its decomposition was accelerated by hydroxylamine. Half-maximum incorporation of 32P in the presence of 10 microM Ca2+ occurred at 60 nM ATP. The calcium-dependent phosphoprotein formation was not affected by 5 mM NaN3, but was inhibited in a dose-dependent fashion by ADP with a 50% inhibition occurring at 180 microM. Fifty mM MgCl2 was required for the maximal phosphorylation. The rate of phosphoprotein decomposition after adding 2 mM EGTA was accelerated by varying the Mg2+ concentration from 10 microM to 3 mM. Alkaline pH (9.0) slowed the rate of phosphoprotein decay. Optimal Ca2+-dependent phosphoprotein occurred at 15 degrees C over a broad pH range (6.4 to 9.0). The activation energy of EGTA-induced phosphoprotein decomposition was 25.6 kcal/mol between 0 and 16 degrees C and 14.6 kcal/mol between 16 and 30 degrees C. The phosphoprotein formed by aortic microsomes was thus quite similar to the acid-stable phosphorylated intermediate of the Ca2+-transport ATPase of sarcoplasmic reticulum from skeletal and cardiac muscle. These data suggest that the Ca2+-dependent phosphoprotein is a reaction intermediate of the Ca2+,Mg2+-ATPase of the aortic microsomes. | lld:pubmed |
| pubmed-article:6151948 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6151948 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6151948 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6151948 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6151948 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:6151948 | pubmed:author | pubmed-author:OkudaHH | lld:pubmed |
| pubmed-article:6151948 | pubmed:author | pubmed-author:SumidaMM | lld:pubmed |
| pubmed-article:6151948 | pubmed:author | pubmed-author:HamadaMM | lld:pubmed |
| pubmed-article:6151948 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6151948 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:6151948 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6151948 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6151948 | pubmed:pagination | 1365-74 | lld:pubmed |
| pubmed-article:6151948 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:6151948 | pubmed:meshHeading | pubmed-meshheading:6151948-... | lld:pubmed |
| pubmed-article:6151948 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6151948 | pubmed:articleTitle | Ca2+,Mg2+-ATPase of microsomal membranes from bovine aortic smooth muscle. Identification and characterization of an acid-stable phosphorylated intermediate of the Ca2+,Mg2+-ATPase. | lld:pubmed |
| pubmed-article:6151948 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6151948 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6151948 | lld:pubmed |
