ADP-RIBOSYLATION OF MYELIN BASIC-PROTEIN BY CHOLERA-TOXIN

被引：5

作者：

ENOMOTO, K ^{[1
]}

ASAKAWA, T ^{[1
]}

机构：

[1] SAGA MED SCH, DEPT PHARMACOL, SAGA 849, JAPAN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1036卷 / 03期

关键词：

MYELIN BASIC PROTEIN; ADP-RIBOSYLATION; CHOLERA TOXIN;

D O I：

10.1016/0304-4165(90)90033-S

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：

Cholera toxin ADP-ribosylates four types of myelin basic proteins (MBPs) of M(r) 14000, 17500, 19000 and 22000 in rat brain myelin. On an analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, MBP underwent mono-and multi-(ADP-ribosyl)ation by cholera toxin and thus modified MBP migrated on the gel as several discrete protein bands, the molecular masses of which were apparently larger by 500-2000 daltons than that of the corresponding untreated MBP. On average, 1.1 mol of ADP-ribosyl residue was incorporated into 1 mol of MBP. Four types of purified MBPs were also ADP-ribosylated by cholera toxin dependent on GTP and the protein factor for the ADP-ribosylation. The results show evidence that MBP is one of major and specific substrates of cholera toxin in brain membranes.

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页码：188 / 192

页数：5

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