Dissociation of proteins from the human 40S ribosomal subunit in a lithium chloride gradient

被引：2

作者：

Malygin, AA ^{[1
]}

Shaulo, DD ^{[1
]}

Karpova, GG ^{[1
]}

机构：

[1] Russian Acad Sci, Novosibirsk Bioorgan Chem Inst, Siberian Div, Novosibirsk 630090, Russia

来源：

MOLECULAR BIOLOGY | 2000年 / 34卷 / 05期

关键词：

human ribosome; disassembly of 40S subunit; ribosomal proteins;

D O I：

10.1007/BF02759619

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：

Human 40S ribosomal subunits were subjected to centrifugation through a 0.3-1.5 M LiCl gradient in 0.5 M KCI, 4 mM MgCl2. Most of the proteins started to dissociate at the initial concentration of monovalent cations (0.8 M); the last to dissociate at 1.55 M salt were the core proteins S3, S5, S7, S10, S15, S16, 817, S19, S20, and S28; among these, S7, S10, S16, and S19 were the most tightly bound to 18S rRNA.

引用

页码：754 / 758

页数：5

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