Activation of membrane-bound high-affinity calcium ion-sensitive adenosine triphosphatase of human erythrocytes by bivalent metal ions
- 1 May 1975
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 147 (2) , 359-361
- https://doi.org/10.1042/bj1470359
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.Keywords
This publication has 11 references indexed in Scilit:
- Dependence on calcium concentration and stoichiometry of the calcium pump in human red cellsThe Journal of Physiology, 1973
- Studies on a Ca2+-dependent ATPase of human erythrocyte membranes: Effects of Ca2+ and H+Biochimica et Biophysica Acta (BBA) - Biomembranes, 1972
- Effects of monovalent cations on the (Mg2+ + Ca2+)-dependent ATPase of the red cell membraneBiochimica et Biophysica Acta (BBA) - Biomembranes, 1971
- Role of bivalent cations in the phosphoglucomutase system. I. Characterization of enzyme-metal complexes.1969
- Structure‐Function Relationships for some Metalloalkaline Phosphatases of E. coliEuropean Journal of Biochemistry, 1969
- The calcium content of human erythrocytesThe Journal of Physiology, 1968
- Enzyme action: views derived from metalloenzyme studies.1968
- The Catalytic and Regulatory Properties of EnzymesAnnual Review of Biochemistry, 1968
- U¨ber das verhalten von adenosintriphosphatasen (ATPasen) in verschiedenen rattenhirnfraktionen unter besonderer beru¨cksichtigung des einflusses mono- und bivalenter kationenBrain Research, 1967
- In vitro Inhibition of Na+-K+ and Mg2+ ATPases by Mono, Di and Trivalent Cations.Experimental Biology and Medicine, 1965