Metabolism of N-acylethanolamine phospholipids by a mammalian phosphodiesterase of the phospholipase D type.
摘要：
Rat heart contains a membrane-bound phosphodiesterase of the phospholipase D type which catalyzes the hydrolysis of 1,2-diacyl-sn-glycero-3-phospho(N-acyl)ethanolamine to N-acylethanolamine and phosphatidic acid. The enzyme also hydrolyzes the corresponding alkenylacylglycerophospho(N-acyl)ethanolamine and N-acylethanolamine lysophospholipids but not phosphatidylcholine or phosphatidylethanolamine. The activity is highest in the microsomal fraction, does not require Ca2+ or Mg2+, and is stimulated by Triton X-100. Bile salts, other ionic detergents, and Zn2+ are inhibitory. Hydrolysis occurs over a wide pH range, with the activity at acid pH being stimulated by freezing and thawing. Other rat tissues also release N-acylethanolamine from N-acylethanolamine phospholipids.
展开
DOI：
10.1016/S0021-9258(17)44667-9
被引量：
年份：
1983
通过文献互助平台发起求助，成功后即可免费获取论文全文。
相似文献
参考文献
引证文献
辅助模式
引用
文献可以批量引用啦~
欢迎点我试用！
