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[枯草杆菌蛋白酶催化精氨酸残基与肽的顺序连接。1. 有机溶剂组成的影响]

[Sequential attachment of arginine residues to peptides, catalyzed by subtilisin. 1. Effect of organic solvent composition].

作者信息

Iusupova M P, Novgorodova S A, Stepanov V M

出版信息

Bioorg Khim. 1996 Jul;22(7):523-7.

PMID:8992957
Abstract

Subtilisin 72 sorbed on a macroporous glass catalyzed the condensation of Dnp(or Z)-Ala2-Leu-OCH3 with arginine amide in a mixture of DMSO and acetonitrile at a water content less than 0.07% (v/v). This reaction resulted in the sequential formation of peptides containing from one to four C-terminal arginine residues. The number of attached Arg residues depended on the DMSO concentration in the solvent mixture, which determined the local arginine excess on the sorbent surface, which significantly exceeded the molar arginine excess in the solution. This enzymic reaction opened up new opportunities for preparation of peptides with different content of arginine residues.

摘要

吸附在大孔玻璃上的枯草杆菌蛋白酶 72 在含水量低于 0.07%(v/v)的二甲基亚砜和乙腈混合物中催化 Dnp(或 Z)-Ala2-Leu-OCH3 与精氨酸酰胺的缩合反应。该反应导致依次形成含有一至四个 C 末端精氨酸残基的肽。连接的精氨酸残基数量取决于溶剂混合物中二甲基亚砜的浓度,这决定了吸附剂表面局部精氨酸的过量情况,该过量情况显著超过溶液中精氨酸的摩尔过量。这种酶促反应为制备具有不同精氨酸残基含量的肽开辟了新的机会。

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