ROLE OF NEGATIVELY CHARGED PHOSPHOLIPIDS IN HIGHLY PURIFIED (NA++K+)-ATPASE FROM RABBIT KIDNEY OUTER MEDULLA .39. STUDIES ON (NA++K+)-ACTIVATED ATPASE
ROLE OF NEGATIVELY CHARGED PHOSPHOLIPIDS IN HIGHLY PURIFIED (NA++K+)-ATPASE FROM RABBIT KIDNEY OUTER MEDULLA .39. STUDIES ON (NA++K+)-ACTIVATED ATPASE
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DOI：
10.1016/0005-2736(78)90092-5
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发表时间：
1978-01-01
期刊：
影响因子：
--
通讯作者：
BONTING, SL
中科院分区：
文献类型：
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作者：
DEPONT, JJHHM;VANPROOIJENVANEEDEN, A;BONTING, SL
1.本文研究了纯化的兔肾外髓（Na ~++ K ~+）ATP酶活性对磷脂极性头部基团的要求。2.微粒体和纯化的酶中磷脂的含量和组成的比较表明，纯化导致磷脂/蛋白质比和磷脂酰丝氨酸含量的增加。3.纯化的制剂每分子（Na ~++ K ~+）-ATP酶含有267个磷脂分子，即95个磷脂酰胆碱、74个磷脂酰乙醇胺、48个鞘磷脂、35个磷脂酰丝氨酸和15个磷脂酰肌醇。4.磷脂酰丝氨酸脱羧酶将磷脂酰丝氨酸完全转化为磷脂酰乙醇胺对纯化制剂的（Na++ K+）-ATP酶活性没有影响。5.磷脂酰肌醇完全水解的磷脂酶C从金黄色葡萄球菌，这是特定的这种磷脂，对（Na++ K+）-ATP酶活性没有影响。6.另一种磷脂酶C（魏氏梭菌）水解95%的磷脂酰胆碱和60- 70%的鞘磷脂和磷脂酰乙醇胺，使（Na++ K+）-ATP酶活性降低约20%。7.磷脂转化酶的组合具有与可以从酶单独的效果计算的效果相同的效果。只有磷脂酰丝氨酸和磷脂酰肌醇两者的完全转化导致44%的（NA++ K+）-ATP酶活性和36%的钾4-硝基苯磷酸酶活性的损失。8.这些实验表明，对极性头基之一没有绝对的要求，尽管在不存在负电荷的情况下，活性低于存在负电荷的情况。
1. The requirement for specific polar head groups of phospholipids for activity of purified (Na++ K+) ATPase from rabbit kidney outer medulla has been investigated. 2. Comparison of content and composition of phospholipids in microsomes and the purified enzyme indicates that purification leads to an increase in the phospholipid/protein ratio and in phosphatidylserine content. 3. The purified preparation contains 267 molecules phospholipid per molecule (Na++ K+)-ATPase, viz. 95 phosphatidylcholine, 74 phosphatidylethanolamine, 48 spingomyelin, 35 phosphatidylserine and 15 phosphatidylinositol. 4. Complete conversion of phosphatidylserine into phosphatidylethanolamine by the enzyme phosphatidylserine decarboxylase has no effect on the (Na++ K+)-ATPase activity of the purified preparation. 5. Complete hydrolysis of phosphatidylinositol by a phospholipase C from Staphylococcus aureus, which is specific for this phospholipid, has no effect on the (Na++ K+)-ATPase activity. 6. Hydrolysis of 95% of the phosphatidylcholine and 60--70% of the spingomyelin and phosphatidylethanolamine by another phospholipase C (Clostridium welchii) lowers the (Na++ K+)-ATPase activity by about 20%. 7. Combination of the phospholipid-converting enzymes has the same effect as can be calculated from the effects of the enzymes separately. Only complete conversion of both phosphatidylserine and phosphatidylinositol results in a loss of 44% of the (NA++ K+)-ATPase activity and 36% of the potassium 4-nitrophenylphosphatase activity. 8. These experiments indicate that there is no absolute requirement for one of the polar head groups, although in the absence of negative charges the activity is lower than in their presence.