[来自微球菌属n的组氨酸脱羧酶马来酰化α链的胰蛋白酶肽段]
[Tryptic peptides of maleylated alpha-chain of histidine decarboxylase from Micrococcus sp. n].
作者信息
Prozorovskiĭ V N, Grebenshchikova O G, Grebenshcikova O G, Rashkovetskiĭ L G
出版信息
Biokhimiia. 1981 Feb;46(2):269-75.
PMID:7248384
Abstract
The maleylated alpha-chain of histidine decarboxylase from Micrococcus sp. n., containing 10 arginine residues was hydrolyzed by trypsin, and 9 peptides were isolated from the tryptic hydrolysate. A comparative study of the amino acid sequence in the tryptic peptides of alpha- and beta-chains of histidine decarboxylase allowed to establish the intramolecular homology in the alpha-chain primary structure and homology between the alpha- and beta-chains.
摘要
来自微球菌属n.的组氨酸脱羧酶的马来酰化α链，含有10个精氨酸残基，被胰蛋白酶水解，从胰蛋白酶水解物中分离出9种肽。对组氨酸脱羧酶α链和β链的胰蛋白酶肽段氨基酸序列进行比较研究，得以确定α链一级结构中的分子内同源性以及α链和β链之间的同源性。
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[Tryptic peptides of maleylated alpha-chain of histidine decarboxylase from Micrococcus sp. n].[来自微球菌属n的组氨酸脱羧酶马来酰化α链的胰蛋白酶肽段]
Biokhimiia. 1981 Feb;46(2):269-75.
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