人胎盘中的氨基肽酶A

S. Mizutani , K. Okano , E Hasegawa , H. Sakura , M. Yamada
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引用次数: 60

摘要

氨基肽酶A (l-α-天冬氨酸(l-α-谷氨酰基)肽水解酶,EC 3.4.11.7)从人胎盘中分离纯化,并与胎盘亮氨酸氨基肽酶进行了简要比较。经胰蛋白酶酶切、sepphacryl S-300层析可分离出氨基酸肽酶A和亮氨酸氨基酸肽酶。用生物学方法证实了人胎盘中氨基肽酶A的血管紧张酶活性(EC 3.4.99.3)。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Aminopeptidase A in human placenta

Aminopeptidase A (l-α-aspartyl(l-α-glutamyl)-peptide hydrolase, EC 3.4.11.7) was found in human placenta, partially purified from it and briefly characterized in comparison with the placental leucine aminopeptidase. The aminopeptidase A could be separated from leucine aminopeptidase after trypsin digestion followed by Sephacryl S-300 chromatography. The angiotensinase (EC 3.4.99.3) activity of aminopeptidase A in human placenta was confirmed by a biological method.

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