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Calcium and magnesium ATPASES of the spectrin fraction of human erythrocytes by F. H. Kirkpatrick; G. M. Woods; P. L. La Celle; R. I. Weed is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Using a rapid method of preparation, spectrin has been isolated from human erythrocytes and its ATPase activity investigated. The ATPase activity with calcium has two distinct components, ‐one with optimal activity when calcium and ATP are of equal concentration (low‐Ca‐ATPase) and another which is activated above 1 mM CaCl~2~ and is maximal at 100 mM CaCl~2~. There is also a Mg‐ATPase with maximal activity at 10 mM MgCl~2~. The high‐Ca‐ATPase of spectrin, but not the low‐Ca‐ATPase, is inhibited by magnesium, while the Mg‐ATPase is inhibited by Ca in excess of ATP. None of these activities exhibits the calcium‐stimulated magnesium‐dependent activity characteristic of the red cell calcium pump.

Who reads Calcium and magnesium ATPASES of the spectrin fraction of human erythrocytes?

Author

F. H. Kirkpatrick; G. M. Woods; P. L. La Celle; R. I. Weed

Publisher

Wiley (John Wiley & Sons); Alan R. Liss, Inc.; Wiley (ISSN 0091-7419)

Published

1975

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)