血管紧张素转换酶（激肽酶II）对缓激肽水解作用的研究。
Studies on the hydrolysis of bradykinin by angiotensin-converting enzyme (kininase II).
作者信息
Dorer F E, Stewart J M, Ryan J W
出版信息
Experientia. 1978 Nov 15;34(11):1436. doi: 10.1007/BF01932334.
PMID:214326
Abstract
Arg-Pro-Pro-Gly-Phe, the N-terminal pentapeptide of bradykinin, is not an inhibitor of angiotensin-converting enzyme and is not hydrolyzed by the enzyme. Arg-Pro-Pro, the N-terminal tripeptide is a relatively potent (IC50 = 2.3 X 10(6) M) inhibitor but its higher homolog. Gly-Arg-Met-Lys-Arg-Pro-Pro is not an inhibitor of angiotensin-converting enzyme.
摘要
缓激肽的N端五肽Arg-Pro-Pro-Gly-Phe不是血管紧张素转换酶的抑制剂，也不被该酶水解。N端三肽Arg-Pro-Pro是一种相对有效的（IC50 = 2.3×10⁻⁶ M）抑制剂，但其更高的同系物Gly-Arg-Met-Lys-Arg-Pro-Pro不是血管紧张素转换酶的抑制剂。
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