Sodium-potassium-activated adenosine triphosphatase. IX. The role of phospholipids.
Sodium-potassium-activated adenosine triphosphatase. IX. The role of phospholipids.
复制标题
钠钾激活的三磷酸腺苷酶。
DOI:
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发表时间:
1973
影响因子:
4.8
通讯作者:
R. Albers
中科院分区:
文献类型:
--
作者:
S. Goldman;R. Albers
Abstract The (Na+ + K+)-ATPase from Electrophorus electroplax was shown to require phospholipids. Treatment of the enzyme with phospholipase A from Naja naja venom removed almost all phosphatides with concomitant loss of enzymatic activity and of the ability to form phosphoryl enzyme. On the other hand digestion with phospholipase C from Clostridium perfringens removed nearly all of the lecithin, two-thirds of the phosphatidylethanolamine, and none of the phosphatidylserine. ATPase activity was partly inhibited by phospholipase C whereas the steady state level of the phosphoryl enzyme and the rate of the Na+-dependent nucleotide transphosphorylation were not impaired. Phospholipase C treatment produced an increased proportion of the E2 conformation at a given level of Mg++; inhibition of the ATPase and p-nitrophenylphosphatase by high Mg++ were more pronounced with the phospholipase C-treated enzyme. The reduced turnover of the phospholipase C-treated ATPase probably arises from this same effect. It was concluded that phosphatidylserine is a requirement for the formation of phosphoryl enzyme as well as its dephosphorylation, and phosphatidylethanolamine acts as a modifier which influences the affinity of the enzyme for Mg++.