Transformation of (Ca2+ + Mg2+)ATPase of calmodulin-depleted erythrocyte membranes into a high Ca2+-affinity form by Ca2+ |
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Authors: | Reinhard Klinger Reinhard Wetzker Inga Fleischer Horst Frunder |
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Institution: | Institute of Physiological Chemistry, University of Jena, DDR-6900 Jena, GDR |
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Abstract: | Specific activity and Ca2+-affinity of (Ca2++Mg2+)ATPase of calmodulin-depleted ghosts progressively increase during preincubation with 0.1–2 mM Ca2+. Concomitantly, the increment in ATPase activity caused by calmodulin and the binding of calmodulin to ghosts decrease. The effects of calcium ions are abolished by the addition of calmodulin. ATP protects the enzyme from a Ca2+-dependent decrease of the maximum activity but does not seem to influence the Ca2+-dependent transformation of the low Ca2+-affinity enzyme into a high Ca2+-affinity form. |
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Keywords: | reprint requests to RK |
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