| pubmed-article:6111625 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C0441833 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C0007448 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C0038734 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C1148926 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
| pubmed-article:6111625 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
| pubmed-article:6111625 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6111625 | pubmed:dateCreated | 1981-6-25 | lld:pubmed |
| pubmed-article:6111625 | pubmed:abstractText | An Mg2+-dependent low ATPase activity can be detected in erythrocyte "white membranes," in addition to that of the well known (Ca2+ + Mg2+)-ATPase. The thiol oxidizing agent diamide affects both activities. The oxidation of neighboring thiols seems to leave the mechanism of the (Ca2+ + Mg2+)-ATPase amplification system evoked by Ca2+ largely unaffected. The perturbation caused by diamide in the membranes seems to affect primarily a step of the ATP hydrolysis mechanism that is common to both ATPase activities. The effectiveness of diamide seems to be the same when either Ca2+ and Mg2+, or Mg2+ alone are present during the reagent action. Reduction of disulfide bonds by DTE after diamide treatment restores the (Ca2+ + Mg2+)-ATPase activity but is unable to take the Mg2+-ATPase activity back to the original level. The hypothesis is discussed that the redox state of one (or more than one) couple of --SH close to each other and possibly connected to the active site, may be an important factor in optimizing the efficiency of Ca action on the (Ca2+ + Mg2+)-ATPase. | lld:pubmed |
| pubmed-article:6111625 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6111625 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6111625 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6111625 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6111625 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6111625 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6111625 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6111625 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6111625 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6111625 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6111625 | pubmed:issn | 0091-7419 | lld:pubmed |
| pubmed-article:6111625 | pubmed:author | pubmed-author:ScutariGG | lld:pubmed |
| pubmed-article:6111625 | pubmed:author | pubmed-author:BallestrinGG | lld:pubmed |
| pubmed-article:6111625 | pubmed:author | pubmed-author:CovazA LAL | lld:pubmed |
| pubmed-article:6111625 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6111625 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:6111625 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6111625 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6111625 | pubmed:pagination | 1-11 | lld:pubmed |
| pubmed-article:6111625 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:meshHeading | pubmed-meshheading:6111625-... | lld:pubmed |
| pubmed-article:6111625 | pubmed:year | 1980 | lld:pubmed |
| pubmed-article:6111625 | pubmed:articleTitle | Divalent cation dependent ATPase activities of red blood cell membranes: influence of the oxidation of membrane thiol groups close to each other. | lld:pubmed |
| pubmed-article:6111625 | pubmed:publicationType | Journal Article | lld:pubmed |
