SYNTHETIC OLIGOPEPTIDE SUBSTRATES WHICH FAIL TO COMPETE WITH H1-HISTONE FOR TYPE-II AND TYPE-III ISOENZYMES OF PROTEIN-KINASE-C

被引：1

作者：

BUDAY, L ^{[1
]}

FARKAS, G ^{[1
]}

FARAGO, A ^{[1
]}

机构：

[1] SEMMELWEIS UNIV,SCH MED,INST BIOCHEM 1,POB 260,H-1444 BUDAPEST 8,HUNGARY

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1992年 / 24卷 / 05期

基金：

匈牙利科学研究基金会;

关键词：

D O I：

10.1016/0020-711X(92)90011-O

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：

1. The oligopeptide AAASFKAKK which contains recognition motifs similar to that found in the surrounding of the site of H1 histone phosphorylated by protein kinase C is unable to compete with H1 histone for the type II and type III isoenzymes, though it is a good substrate for protein kinase C and it is able to compete with a physiological substrate of the enzyme. 2. Among several oligopeptides tested as an alternative substrate a very basic peptide proved to be the most effective inhibitor of H1 histone phosphorylation. This oligopeptide substrate contains basic recognition motifs at both sides of the phosphorylated residue at variance with the sequence of H1 histone in the surrounding of the phosphorylated site.

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页码：777 / 782

页数：6

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