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Biochim Biophys Acta ; 633(2): 299-304, 1980 Dec 01.
Artigo em Inglês | MEDLINE | ID: mdl-6109550

RESUMO

The effect of purified calmodulin on the calcium-dependent phosphorylation of human erythrocyte membranes was studied. Under the conditions employed, only one major peak of phosphorylation was observed when solubilized membrane proteins were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight of this phosphorylated protein band was estimated to be 130000 and in the presence of purified red blood cell calmodulin, the rate of phosphorylation of this band was increased. These data suggest that calmodulin activation of (Ca2+ + Mg2+)-ATPase could be a partial reflection of an increased rate of phosphorylation of the (Ca2+ + Mg2+)-ATPase of human erythrocyte membranes.


Assuntos
Proteínas de Ligação ao Cálcio/farmacologia , ATPases Transportadoras de Cálcio/metabolismo , Calmodulina/farmacologia , Membrana Eritrocítica/enzimologia , Eritrócitos/enzimologia , ATPase de Ca(2+) e Mg(2+) , Cálcio/farmacologia , Eletroforese em Gel de Poliacrilamida , Ativação Enzimática , Membrana Eritrocítica/efeitos dos fármacos , Humanos , Peso Molecular , Fosforilação , Sódio/farmacologia
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