通过一种膜结合的大鼠肝脏甲硫氨酸氨肽酶从血红蛋白新生肽中去除N端甲硫氨酸。
Removal of N-terminal methionine from haemoglobin nascent peptides by a membrane-bound rat liver methionine aminopeptidase.
作者信息
Termignoni C, Freitas J O, Guimarães J A
出版信息
Biochem J. 1986 Mar 1;234(2):469-73. doi: 10.1042/bj2340469.
Abstract
A membrane-bound aminopeptidase able to remove methionine from haemoglobin nascent peptides is described. The enzyme also hydrolyses methionine from methionyl-lysyl-bradykinin but not lysine from lysyl-bradykinin. The tripeptide Met-Ala-Ser is poorly hydrolysed. This aminopeptidase also splits amino acid 2-naphthylamides, being, however, less specific with respect to these synthetic substrates.
摘要
描述了一种能够从血红蛋白新生肽中去除甲硫氨酸的膜结合氨肽酶。该酶还能从甲硫氨酰 - 赖氨酰 - 缓激肽中水解甲硫氨酸，但不能从赖氨酰 - 缓激肽中水解赖氨酸。三肽甲硫氨酸 - 丙氨酸 - 丝氨酸水解程度较低。这种氨肽酶也能裂解氨基酸2 - 萘酰胺，然而，对于这些合成底物，其特异性较低。
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引用本文的文献
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Mol Cell Biochem. 1991 Apr 10;102(2):101-13. doi: 10.1007/BF00234568.
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