SUSCEPTIBILITY TO TRYPTIC HYDROLYSIS OF PEPTIDE-BONDS INVOLVING EPSILON-N-METHYLLYSINE

被引：12

作者：

JOYS, TM

KIM, H

机构：

[1] The Department of Microbiology, Texas Tech Health Sciences Center at Lubbock, Lubbock

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 581卷 / 02期

基金：

美国国家卫生研究院;

关键词：

(S. typhimurium); N-Methyllysine; Peptide bond; Tryptic hydrolysis;

D O I：

10.1016/0005-2795(79)90256-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Using isolation of soluble peptides as a means of comparing the efficiency of tryptic hydrolysis of various forms of the phase-1 flagellin of Salmonella typhimurium, it was found that peptides terminating in N-methyllysine required a longer period of exposure to enzyme for their detection than did equivalent peptides terminating in lysine. © 1979.

引用

页码：360 / 362

页数：3

共 14 条

[1]

ANDREWS FW, 1922, J PATHOL BACTERIOL, V25, P515

[2] HYDROLYSIS OF TWO EPSILON-N-METHYL-L-LYSINE DERIVATIVES BY TRYPSIN [J].