PURIFICATION AND PROPERTIES OF A HISTONE ACETYLTRANSFERASE FROM ARTEMIA-SALINA, HIGHLY EFFICIENT WITH H1-HISTONE

被引：18

作者：

CANO, A ^{[1
]}

PESTANA, A ^{[1
]}

机构：

[1] UNIV AUTONOMA MADRID, FAC MED,DEPT BIOQUIM,MED, INST ENZIMOL & PATOL MOLEC, MADRID 34, SPAIN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 97卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1979.tb13086.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：

An histone acetyltransferase has been purified from nuclei of 40‐h‐old Artemia salina larvae. The enzyme is very unstable at 0°C, requires free − SH groups for activity and is rapidly inactivated at 40°C. The optimal pH for activity is 8.5 and the activity is half inhibited by millimolar concentrations of Mn2+, Ca2+ or Mg2+ or decimolar concentrations of Na+ and K+. The molecular weight of the enzyme, determined by gel filtration chromatography, changed with the ionic strength of the medium (280000 in 10 mM Tris · HCl, 170000 in 0.2 M KCl). The very‐lysine‐rich histone H1 is a better substrate acceptor than the arginine‐rich histones H3 or H4. Under proper conditions, the enzyme can modify all the internal lysyl residues in histones H1 and H4. The acetylation of H1 is inhibited when all the other histone fractions are present in the assay mixture. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：65 / 72

页数：8

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