PMID: 126684May 1, 1975

Activation of membrane-bound high-affinity calcium ion-sensitive adenosine triphosphatase of human erythrocytes by bivalent metal ions

The Biochemical Journal
H Pfleger, H U Wolf

Abstract

The Ca2+-sensitive ATPase (adenosine triphosphatase) of human erythrocyte membranes is activated, not only by Ca2+ ions, but also by a series of other bivalent metal ions including Sr2+, Ba2+, Mn2+, Ni2+, Co2+, Cd2+, Cu2+, Zn2+ and Pb2+. The degree of activation is dependent on the radius of the ion rather than on its nature, in contrast with the dissociation constant of the enzyme--metal ion complex.

Citations

Mar 4, 2003·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·J F StaubA M Perault-Staub
May 13, 2017·International Journal of Molecular Sciences·Sarah E Orr, Christy C Bridges
Jul 9, 1984·FEBS Letters·T J Simons
Nov 1, 1990·Environmental Health Perspectives·M A Verity
Jul 1, 1981·The Histochemical Journal·J A Firth, G J Stranks

Related Concepts

DNA-dependent ATPase
Calcium
Plasma Membrane
Enzyme Activation
Erythrocytes
Mercury

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