ENZYME COUPLING METHOD ON CALIBRATED NYLON SPHERES - APPLICATION TO THE SELECTIVE TRYPSINIZATION OF HISTONES IN CHROMATIN

被引：19

作者：

MICHALON, P

COUTURIER, R

HACQUES, MF

FAVREBONVIN, G

VILLE, A

MARION, C

机构：

[1] UNIV LYON 1,PHYS CHIM BIOL LAB,CNRS,LBTM,UM 24,43 BD 11 NOVEMBRE 1918,F-69622 VILLEURBANNE,FRANCE

[2] UNIV LYON 1,BIOCHIM APPL LAB,F-69622 VILLEURBANNE,FRANCE

[3] UNIV LYON 1,BIOCHIM ANALYT LAB,CNRS,UA 244,F-69622 VILLEURBANNE,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 167卷 / 01期

关键词：

D O I：

10.1016/0006-291X(90)91722-5

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 new method consisting of a two-step activation was developed in order to covalently immobilize enzymes on calibrate nylon 66 spheres. This efficient method associates for the first time peptide bond cleavage and O-alkylation of the support. Optimal conditions for activation and protein coupling were defined, and immobilized trypsin was used to investigate the histone accessibility on chromatin. This approach, which allows us to degrade first progressively H1, indicates that H4 seems inaccessible both in relaxed and condensed chromatin. © 1990.

引用

页码：9 / 15

页数：7

共 23 条

[1] A SIMPLE METHOD FOR THE ESTIMATION OF AMINO-GROUPS ON INSOLUBLE MATRIX BEADS [J].