PARTIAL-PURIFICATION OF 2 PROTEINS WHICH SENSITIZE RIBOSOMES TO GELONIN - SENSITIZATION IS NOT LINKED TO PHOSPHORYLATION OF RIBOSOMAL-PROTEINS

被引：5

作者：

BRIGOTTI, M ^{[1
]}

SPERTI, S ^{[1
]}

CARNICELLI, D ^{[1
]}

MONTANARO, L ^{[1
]}

机构：

[1] UNIV BOLOGNA, DIPARTIMENTO PATOL SPERIMENTALE, VIA SAN GIACOMO 14, I-40126 BOLOGNA, ITALY

来源：

TOXICON | 1993年 / 31卷 / 08期

关键词：

D O I：

10.1016/0041-0101(93)90258-K

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Inactivation of ribosomes by gelonin, from Gelonium multiflorum, requires ATP and extraribosomal protein(s) present in the rabbit reticulocyte lysate [SPERTI, S. et al. (1991) Biochem. J. 277, 281-284]. On the anion exchanger Mono Q the activity responsible for the sensitization of ribosomes to gelonin resolves in two peaks which both display a kinase activity on ribosomal proteins. However, staurosporin, an inhibitor of several protein kinases, strongly inhibits phosphorylation of ribosomal proteins without affecting the gelonin-promoting activity of Mono Q peaks. All the evidence collected contradicts a direct link between sensitization to gelonin and phosphorylation of ribosomes.

引用

页码：989 / 996

页数：8

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