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KMID : 0376219750120020397
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Chonnam Medical Journal
1975 Volume.12 No. 2 p.397 ~ p.403
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Membrane Ca^(2+)-dependent Adenosine Triphosphatase in Chicken Erythrocytes
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Abstract
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The properties of membrane-bound Ca2+-dependent adenosine triphosphatase (Ca2+-ATPase) were studied with intact chicken erythrocytes.
The enzyme required Ca2+ and Mg2+, being activated markedly by Ca2+andMg2+.
The enzyme showed.a sharp optimum pH at 7.0, and was found to be unrelated
to the Nal-K+-stimulated ATPase, being not influenced by Na+, K+ and oubain. The enzyme acted upon ATP, CTP and UTP with almost equal rates.
The incubation of intact erythrocytes with each of trypsin, lipase and phospholipase C resulted in decreased enzyme activity, suggesting that the enzyme is anecto-enzyme, i.e. enzyme on the plasma membrane with its active site facing theexternal medium.
The enzyme activity was enhanced 2-fold by 1 mM sodium deoxycholate and sodium dodecylsuifate.
These results suggest that ecto-Ca2+-ATPase of chicken erytbocytes exists as a phospholipid-protein complex at the external site of the plasma membrane.
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