从大鼠肾脏中纯化的一种羧肽酶样酶对内皮素-1的快速失活作用。
Rapid inactivation of endothelin-1 by a carboxypeptidase-like enzyme purified from rat kidney.
作者信息
Jeng A Y, Deng Y
机构信息
Research Department, Ciba-Geigy Corp., Summit, New Jersey 07901.
出版信息
J Cardiovasc Pharmacol. 1993;22 Suppl 8:S69-72. doi: 10.1097/00005344-199322008-00020.
A survey of various rat tissues showed that the kidney had the highest endothelin degradation enzyme activity. An enzyme that effectively inactivated endothelin-1 was purified from soluble kidney extracts. This enzyme appeared to contain two subunits with molecular weights of 34 kDa and 21 kDa. It displayed carboxypeptidase-like properties and cleaved off the carboxyl terminal tryptophan of endothelin-1. These results agree with the findings that endothelin-1 is cleared efficiently by the kidney and suggest that this enzyme plays a role in the homeostasis of circulating endothelin-1.
对多种大鼠组织进行的一项调查显示，肾脏具有最高的内皮素降解酶活性。从肾脏可溶性提取物中纯化出一种能有效使内皮素-1失活的酶。这种酶似乎含有两个亚基，分子量分别为34 kDa和21 kDa。它表现出类羧肽酶的特性，并能切割掉内皮素-1的羧基末端色氨酸。这些结果与内皮素-1被肾脏有效清除的研究结果一致，并表明这种酶在循环内皮素-1的稳态中发挥作用。
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