| pubmed-article:1836790 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1836790 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:1836790 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:1836790 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:1836790 | lifeskim:mentions | umls-concept:C0332479 | lld:lifeskim |
| pubmed-article:1836790 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:1836790 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:1836790 | lifeskim:mentions | umls-concept:C0205266 | lld:lifeskim |
| pubmed-article:1836790 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1836790 | pubmed:dateCreated | 1992-2-4 | lld:pubmed |
| pubmed-article:1836790 | pubmed:abstractText | Intact human erythrocytes, initially depleted of Mg2+ by EDTA incubation in the presence of A23187, exhibit Mg(2+)-dependent phosphate production of around 1.5 mmol per liter cells.h, half-maximally activated at around 0.4 mM added free Mg2+. This appears to correspond to Mg(2+)-stimulated adenosine triphosphatase (Mg(2+)-ATPase) activity found in isolated membranes, which is known to have a similar activity and affinity for Mg2+. Vanadate (up to 100 microM) inhibited Mg(2+)-dependent phosphate production and ATP breakdown in intact cells. Over a similar concentration range vanadate (3-100 microM) transformed intact cells from normal discocytes to echinocytes within 4-8 h at 37 degrees C, and more rapidly in Mg(2+)-depleted cells. The rate of Ca(2+)-induced echinocytosis was also enhanced in Mg(2+)-depleted cells. These results support previous studies in erythrocyte ghosts suggesting that vanadate-induced shape change is associated with inhibition of Mg(2+)-ATPase activity localized in the plasma membrane of the red blood cell. | lld:pubmed |
| pubmed-article:1836790 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1836790 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1836790 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1836790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1836790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1836790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1836790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1836790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1836790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1836790 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1836790 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1836790 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1836790 | pubmed:issn | 0730-2312 | lld:pubmed |
| pubmed-article:1836790 | pubmed:author | pubmed-author:RoufogalisB... | lld:pubmed |
| pubmed-article:1836790 | pubmed:author | pubmed-author:LuZ YZY | lld:pubmed |
| pubmed-article:1836790 | pubmed:author | pubmed-author:YUY GYG | lld:pubmed |
| pubmed-article:1836790 | pubmed:author | pubmed-author:ConigraveA... | lld:pubmed |
| pubmed-article:1836790 | pubmed:author | pubmed-author:AulandM EME | lld:pubmed |
| pubmed-article:1836790 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1836790 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:1836790 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1836790 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1836790 | pubmed:pagination | 284-90 | lld:pubmed |
| pubmed-article:1836790 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1836790 | pubmed:meshHeading | pubmed-meshheading:1836790-... | lld:pubmed |
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| pubmed-article:1836790 | pubmed:meshHeading | pubmed-meshheading:1836790-... | lld:pubmed |
| pubmed-article:1836790 | pubmed:meshHeading | pubmed-meshheading:1836790-... | lld:pubmed |
| pubmed-article:1836790 | pubmed:meshHeading | pubmed-meshheading:1836790-... | lld:pubmed |
| pubmed-article:1836790 | pubmed:meshHeading | pubmed-meshheading:1836790-... | lld:pubmed |
| pubmed-article:1836790 | pubmed:meshHeading | pubmed-meshheading:1836790-... | lld:pubmed |
| pubmed-article:1836790 | pubmed:meshHeading | pubmed-meshheading:1836790-... | lld:pubmed |
| pubmed-article:1836790 | pubmed:meshHeading | pubmed-meshheading:1836790-... | lld:pubmed |
| pubmed-article:1836790 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1836790 | pubmed:articleTitle | Association of vanadate-sensitive Mg(2+)-ATPase and shape change in intact red blood cells. | lld:pubmed |
| pubmed-article:1836790 | pubmed:affiliation | Department of Biochemistry, University of Sydney, New South Wales, Australia. | lld:pubmed |
| pubmed-article:1836790 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1836790 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1836790 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1836790 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1836790 | lld:pubmed |
