CHARACTERIZATION OF HISTONE CORE COMPLEX

被引：54

作者：

CHUNG, SY ^{[1
]}

HILL, WE ^{[1
]}

DOTY, P ^{[1
]}

机构：

[1] UNIV MONTANA,DEPT CHEM,MISSOULA,MT 59812

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1978年 / 75卷 / 04期

关键词：

D O I：

10.1073/pnas.75.4.1680

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

A stable histone core complex containing equimolar ratios of H2A, H2B, H3, and H4 has been isolated from chicken erythrocyte chromatin in high salt. This complex has been characterized by sedimentation and chemical cross-linking studies. In velocity ultracentrifugation, only one single sharp sedimentation boundary has been observed with sedimentation coefficient S20,w0 = 3.8±0.1. The molecular weight of the histone core complex has been investigated by low-speed sedimentation equilibrium studies over a wide range of protein concentration. Analysis of the apparent weight-average molecular weight as a function of concentration indicates that the histone core complex in 2 M NaCl, pH 9.0 is in equilibrium between a tetramer (H2A)(H2B)(H3)(H4) and an octamer [(H2A)(H2B)(H3)(H4)]2 species with a tetramer molecular weight of 55,000. The equilibrium constant K is approximately 1.2 x 10-5 liter per mol at 10°. Evidence of such a tetramer-octamer equilibrium in solution is also supported by the results of our chemical crosslinking experiments on the histone core complex.

引用

页码：1680 / 1684

页数：5

共 32 条

[1]

Adams ET, 1963, ULTRACENTRIFUGAL ANA, P119

[2]

ADAMS ET, 1965, BIOCHEMISTRY, V8, P1646

[3] NUCLEASE CLEAVAGE OF CHROMATIN AT 100-NUCLEOTIDE PAIR INTERVALS [J].