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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 S...

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Detalles Bibliográficos
Autores principales: Cha, Young N., Shin, Bak C., Lee, Kwang S.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1971
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2203076/
https://www.ncbi.nlm.nih.gov/pubmed/5543418
Descripción
Sumario: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 (Ca(++) ATPase) and Ca(++) uptake of RBCMF were studied. It was found that pretreatment of RBCMF at 50°C abolished both Ca(++) ATPase and Ca(++) uptake. Pretreatment of RBCMF with phospholipases A and C decreased both Ca(++) ATPase and Ca(++) uptake, whereas pretreatment with phospholipase D did not significantly alter either Ca(++) ATPase or Ca(++) uptake. Both Ca(++) ATPase and Ca(++) uptake had ATP specificity, similar optimum pH's, and optimum incubation temperatures. From these results, it was concluded that Ca(++) uptake is intimately linked to Ca(++) ATPase.