Active Uptake of Ca++ and Ca++-Activated Mg++ ATPase in Red Cell Membrane Fragments

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Active Uptake of Ca++ and Ca++-Activated Mg++ ATPase in Red Cell Membrane Fragments

Isolated human red blood cell membrane fragments (RBCMF) were found to take up Ca(++) in the presence of ATP.(1) This ATP-dependent Ca(++) uptake by RBCMF appears to be the manifestation of an active Ca(++) transport mechanism in the red cell membrane reported previously (Schatzmann, 1966; Lee and Shin, 1969). The influences of altering experimental conditions on Ca(++)-stimulated Mg(++) ATPase...

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The membrane ATPase of the (Mg, Ca)-ATPase-mutant E. coli K 12, strain AN 120.

In the (Mg,Ca)-ATPase-mutant E.coli K 12 strain AN 120, isolated by Butlin et a l.1, the acti­ vity of the membrane ATPase and of the ATPdependent transhydrogenase2 is greatly reduced. These cells are not able to grow on succinate or D-lactate because they lack oxidative phosphoryla­ tion. In the course of testing the properties of mem­ brane ATPase, we found, in addition to the reduc­ tion of ...

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Plasma membrane Ca(2+)-ATPase sulfhydryl modifications: implication for oxidized red cell.

A common perturbation found in cells under oxidative stress is alteration in cellular Ca2+ homeostasis. In order to understand the effects of such oxidative damage, human red cell plasma membrane Ca(2+)-ATPase (PMCA) was studied by measuring PMCA activity, both in the presence and absence of calmodulin (CaM), following treatment with sulfhydryl agents, N-ethylmaleimide, iodoacetate and diamide....

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Ca ” ’ + Mg 2 + ) - ATPase Activity in Plasma Membrane of Circulating Mononuclear Cells

The in vivo effect of vitamin D on (Ca2+ + Mg2+)ATPase activity was examined in a plasma membrane fraction of rat circulating mononuclear cells (MPM). Although there was no significant difference in the ATPase activities in red blood cell ghosts, (Ca”’ + Mg2+)-ATPase activity in MPM was significantly higher (p < 0.05) in long-term vitamin DB-replete rats (100 IU/day for 6 months) than that in v...

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Inhibition of Mg, Ca-ATPase from E. coli by ruthenium red.

The membrane-bound, solubilized, and trypsin-treated forms of Mg, Ca-ATPase from E. coli are inhibited by ruthenium red [RR]. The inhibition is noncompetitive and is reduced at higher substrate concentrations. n-Butanol-extracted ATPase is not inhibited by ruthenium red and is not activated by KCl.

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ژورنال

عنوان ژورنال: Journal of General Physiology

سال: 1971

ISSN: 1540-7748,0022-1295

DOI: 10.1085/jgp.57.2.202