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PMID: 5543418 Published · ppublish English Journal Article

Active uptake of Ca++ and Ca plus,plus-activated Mg++ ATPase in red cell membrane fragments.

The Journal of general physiology ·Vol. 57 ·No. 2 ·1971-02-00 ·Pages 202-15

Cha YN, Shin BC, Lee KS

Abstract

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 degrees 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.

MeSH Terms
Adenosine Triphosphate/metabolism,pharmacology Biological Transport, Active/drug effects Calcium/metabolism,pharmacology Calcium Isotopes Cell Membrane/metabolism
Chemicals
Calcium Isotopes Adenosine Triphosphate Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cha Y N
Shin B C
Lee K S
References (9)
9 references, click to expand
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    J Gen Physiol. 1969 Dec;54(6):713-29 PMID: 5357189
  8. Inside-out red cell membrane vesicles: preparation and purification.
    Science. 1970 Apr 10;168(3928):255-7 PMID: 5418644
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Article Info
Journal
The Journal of general physiology
Abbr.
J Gen Physiol
ISSN
0022-1295
Published
1971-02-00
Pages
202-15
Language
English
Region
United States
NLM ID
2985110R
PMCID
PMC2203076
Subset
IM
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