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Calcium and magnesium ATPASES of the spectrin fraction of human erythrocytes

✍ Scribed by Kirkpatrick, F. H. ;Woods, G. M. ;La Celle, P. L. ;Weed, R. I.

Publisher
Wiley (John Wiley & Sons)
Year
1975
Tongue
English
Weight
672 KB
Volume
3
Category
Article
ISSN
0091-7419

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✦ Synopsis

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.

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Method for the preparation of human eryt
Method for the preparation of human erythrocyte membrane with low basal calcium ATPase, responsive to stimulation
✍ J.H. Thakar 📂 Article 📅 1985 🏛 Elsevier Science 🌐 English ⚖ 307 KB

A simple procedure for preparing erythrocyte membranes with low basal Ca2+ ATPase activity is described, which is stimulated several-fold by the addition of hemolysate in the incubation mixture. The cells are hemolyzed in hypotonic imidazole buffer and resulting membranes are washed with hypotonic p