PURIFICATION AND CHARACTERIZATION OF THE MAJOR 50-KDA REPRESSOR PROTEIN FROM CYTOPLASMIC MRNP OF RABBIT RETICULOCYTES

被引：78

作者：

MINICH, WB ^{[1
]}

MAIDEBURA, IP ^{[1
]}

OVCHINNIKOV, LP ^{[1
]}

机构：

[1] RUSSIAN ACAD SCI, INST PROT RES, PUSHCHINO 142292, RUSSIA

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1993年 / 212卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1993.tb17701.x

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：

A 50-kDa protein has been purified to homogeneity from free mRNP of rabbit reticulocytes. This protein, designated as p50, is present within both free mRNP (approximately 4 mol protein/mol globin mRNA) and polyribosomal mRNP (approximately 2 mol protein/mol globin mRNA). p50 is a basic protein (pl almost-equal-to 9.5) and is characterized by a high glycine content of approximately 20%. Nitrocellulose-filter analysis has shown that p50 interacts with globin mRNA with an association constant of approximately 2.5 x 10(8) m-1 (100 mM KAc, 4-degrees-C). Various RNA and polyribonucleotides have the following relative affinity for p50; poly(G) > poly(U) > globin mRNA almost-equal-to 16S rRNA > poly(A) > poly(C). p50 can be phosphorylated both in vitro and in vivo.

引用

页码：633 / 638

页数：6

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