{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,8]],"date-time":"2023-10-08T06:40:01Z","timestamp":1696747201666},"reference-count":23,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2006,7,11]],"date-time":"2006-07-11T00:00:00Z","timestamp":1152576000000},"content-version":"vor","delay-in-days":7710,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American J Hematol"],"published-print":{"date-parts":[[1985,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The effect of the thiol\u2010oxidizing agent diamide on erythrocyte (Ca<jats:sup>+2<\/jats:sup>+Mg<jats:sup>+2<\/jats:sup>)\u2010ATPase activity was measured in normal and glucose\u20106\u2010phosphate\u2010dehydrogenase\u2010deficient (G6PD<jats:sup>\u2212<\/jats:sup>) cells. Although the enzyme activity before the oxidative stress was similar in both groups, diamide induced a markedly greater inhibition in the enzyme activity in the G6PD<jats:sup>\u2212<\/jats:sup> cells than in the normal controls. These data indicate dependence of erythrocyte (Ca<jats:sup>+2<\/jats:sup>+Mg<jats:sup>+2<\/jats:sup>)\u2010ATPase, in part, on the redox status of the cell. The increased vulnerability of (Ca<jats:sup>+2<\/jats:sup>+Mg<jats:sup>+2<\/jats:sup>)ATPase to oxidative stress in G6PD<jats:sup>\u2212<\/jats:sup> may be of pathophysiological relevance to their premature destruction in oxidant\u2010induced hemolysis.<\/jats:p>","DOI":"10.1002\/ajh.2830190204","type":"journal-article","created":{"date-parts":[[2007,2,21]],"date-time":"2007-02-21T09:58:55Z","timestamp":1172051935000},"page":"131-136","source":"Crossref","is-referenced-by-count":8,"title":["Erythrocyte (Ca<sup>+2<\/sup>+Mg<sup>+2<\/sup>)\u2010ATPase activity: Increased sensitivity to oxidative stress in glucose\u20106\u2010phosphate dehydrogenase deficiency"],"prefix":"10.1002","volume":"19","author":[{"given":"Oded","family":"Shalev","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vardiella","family":"Lavi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert P.","family":"Hebbel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John W.","family":"Eaton","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2006,7,11]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1085\/jgp.54.1.123"},{"key":"e_1_2_1_3_2","first-page":"128","article-title":"Interactions of complement with the red cell membrane","volume":"16","author":"Rosse WF","year":"1979","journal-title":"Semin Hematol"},{"key":"e_1_2_1_4_2","first-page":"341","article-title":"Genetic Disorders of glutathione and sulfur amino\u2014acid metabolism. 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