Purification of a high-molecular-mass form of phospholipase A2 from rat kidney activated at physiological calcium concentrations.
Purification of a high-molecular-mass form of phospholipase A2 from rat kidney activated at physiological calcium concentrations.
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从在生理钙浓度下激活的大鼠肾脏中纯化高分子量形式的磷脂酶 A2。
DOI：
10.1042/bj2710037
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
Nemenoff,RA
中科院分区：
文献类型：
--
作者：
Gronich,JH;Bonventre,JV;Nemenoff,RA
大鼠肾脏含有可溶性磷脂酶A2（PLA 2），其在色谱上与之前在大鼠肾系膜细胞中鉴定的激素调节形式的酶相同。这种肾酶已被纯化的连续柱分馏。纯化的酶是一个110 kDa的多肽，可以水解花生四烯酸磷脂酰胆碱和花生四烯酸磷脂酰乙醇胺，但对花生四烯酸磷脂酰肌醇的活性低。该酶是相当大的比大多数以前分离的形式的分泌或细胞内的PLA 2，并刺激生理浓度的Ca 2+，在500 nM-Ca 2+的半最大激活发生。这种酶的激素调节和Ca 2（+）依赖性强烈表明，它在肾脏中花生四烯酸的释放和前列腺素的产生中起着重要的作用。
Rat kidney contains a soluble phospholipase A2 (PLA2), which is chromatographically identical with a previously identified hormonally regulated form of the enzyme in rat renal mesangial cells. This kidney enzyme has been purified by sequential column fractionation. The purified enzyme is a 110 kDa polypeptide which can hydrolyse arachidonoyl phosphatidylcholine and arachidonoyl phosphatidylethanolamine, but has low activity towards arachidonoyl phosphatidylinositol. The enzyme is considerably larger than most previously isolated forms of secretory or intracellular PLA2, and is stimulated by physiological concentrations of Ca2+, with half-maximal activation occurring at 500 nM-Ca2+. The hormonal regulation and Ca2(+)-dependency of this enzyme strongly suggest that it plays a role in hormonally regulated arachidonic acid release and prostaglandin production in the kidney.
大鼠肾脏中的磷脂酶 A2
影响因子：
2.8
作者：
B. Baggio;S. Favaro;A. Antonello;A. Bonn;A. Borsatti
通讯作者：
A. Borsatti