INFLUENCE OF UREA ON ELECTROPHORETIC PROPERTIES OF PROTEINS OF MICROSOMAL MEMBRANES

被引：13

作者：

BERKMAN, PM

PASTEWKA, JV

PEACOCK, AC

机构：

[1] Chemistry Branch, National Cancer Institute, National Institutes of Health, Bethesda

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 181卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0005-2795(69)90236-0

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：

Proteins of the membranes portion of the endoplasmic reticulum may be solubilized and separated into 15 bands by disc electrophoresis. The separation depends on the presence of urea in the gel. With no urea present, fewer than 4 bands were observed. Bands which appeared homogeneous in the absence of urea dispersed when reelectrophoresed in its presence. After protein fractionation in the presence of urea, the separated proteins migrated with approximately the same mobility in the absence of urea. © 1969.

引用

页码：159 / &

共 16 条

[1]

BARTLETT GR, 1959, J BIOL CHEM, V234, P466

[2]

BLIGH EG, 1959, CAN J BIOCHEM PHYS, V37, P911

[3] STUDIES ON FREE AND MEMBRANE-BOUND RIBOSOMES IN RAT LIVER .I. DISTRIBUTION AS RELATED TO TOTAL CELLULAR RNA [J].