descriptionPublicationkeyboard_double_arrow_right Article , Other literature type 01 Jan 1979 English Publisher:S. Karger AGJournal:Enzyme, volume 24, pages 374-382 (issn: 0013-9432, eissn: 2504-2564,

Authors: M Kodícek; M Kotva; H Rehácková; L Mircevová;

doi: 10.1159/000458693

pmid: 160314

Activation of Mg-ATPase (Spectrin-Dependent ATPase) by Ca^2+

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Abstract

The dependence of saponin-stimulated Mg-ATPase activity in the erythrocyte membrane on Ca2+ concentration was studied. In the membrane of freshly sampled human erythrocytes we found for this enzyme and Ca2+ an apparent dissociation constant of 0.611 mumol/l (SE +/- 0.106 mumol/l) and Hill coefficient of 0.93 (SE +/- 0.05). The enzyme is in most probability identical with Ca,Mg-ATPase of high affinity to Ca2+ described also as spectrin-dependent Ca,Mg-ATPase.

Keywords

Adenosine Triphosphatases, Erythrocyte Membrane, Membrane Proteins, Spectrin, Saponins, Enzyme Activation, Kinetics, Humans, Calcium, Magnesium

3 Research products, page 1 of 1

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