三肽基羧基肽酶活性(血管紧张素转换酶)

Jin-Ichi Inokuchi, Atsuo Nagamatsu
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引用次数: 47

摘要

高纯化猪肺肾动激酶II(血管紧张素转换酶)制剂降解脱氧- arg9 -缓激肽及其类似物的研究对肽基二肽水解酶(ec3.4.15.1)进行了研究。采用高效液相色谱法对降解肽片段进行分离和氨基酸鉴定。这两种酶释放的c端三肽分别为:des-Arg9-缓激肽、des-Arg9-(Leu8)-缓激肽、Pro-Pro-Gly-Phe-Ser-Pro-Phe、Pro-Gly-Phe-Ser-Pro-Phe、Gly-Phe-Ser-Pro-Phe、Bz-Gly-Ser-Pro-Phe和Bz-Gly-Ala-Pro-Phe。这两种酶对Phe-Ser-Pro-Phe、Bz-Gly-His-Pro-Phe、bz - gly - phe和Bz-Gly-Gly-Pro-Phe的水解均可忽略不计。这些数据表明,kininase II可以释放具有脯氨酸残基的底物的c端三肽,如des-Arg9-bradykinin及其类似物,并且该酶不仅可以作为二肽基羧肽酶,还可以作为三肽基羧肽酶。该酶的三肽基羧肽酶活性对激酶II抑制剂的抑制很敏感。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Tripeptidyl carboxypeptidase activity of kininase II (angiotensin-converting enzyme)

The degradation of des-Arg9-bradykinin and its analogues by highly purified preparations of hog lung and kidney kininase II (angiotensin-converting enzyme; peptidyldipeptide hydrolase, EC 3.4.15.1) was studied. The degradative peptide fragments were separated and isolated by high performance liquid chromatography and identified by amino acid analysis. Both enzymes released C-terminal tripeptides from des-Arg9-bradykinin, des-Arg9-(Leu8)-bradykinin, Pro-Pro-Gly-Phe-Ser-Pro-Phe, Pro-Gly-Phe-Ser-Pro-Phe, Gly-Phe-Ser-Pro-Phe, Bz-Gly-Ser-Pro-Phe and Bz-Gly-Ala-Pro-Phe. Hydrolysis of Phe-Ser-Pro-Phe, Bz-Gly-His-Pro-Phe, Bz-Gly-Phe-Pro-Phe and Bz-Gly-Gly-Pro-Phe by both enzymes was negligible. These data indicate that kininase II can release C-terminal tripeptides of substrates having a proline residue in the penultimate position such as des-Arg9-bradykinin and its analogues, and that this enzyme is able not only to act as a dipeptidyl carboxypeptidase but also acts as a tripeptidyl carboxypeptidase. The tripeptidyl carboxypeptidase activity of this enzyme was sensitive to inhibition by kininase II inhibitors.

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