Analysis by two-dimensional polyacrylamide gel electrophoresis of the in vivo phosphorylation of ribosomal proteins derived from free and membrane-bound polysomes.

Abstract:

:Analysis of in vivo phosphorylation of mouse liver ribosomal proteins was performed by two-dimensional polyacrylamide gel electrophoresis following 32P-injection. Our method is special and differs from other eukaryotic systems reported in that all proteins separated on the first dimension gel are completely solubilized, moving quantitatively to the second dimension gel. Only ribosomes from polysomes were used, ensuring analysis of ribosomes actively engaged in protein synthesis. We resolved sixty-five distinct proteins from ribosomes from membrane bound or free polysomes. In both cases radioautography revealed similar labeled patterns with one highly phosphorylated ribosomal protein and five marginally labeled spots.

journal_name

Mol Biol Rep

authors

Hoffman WL,Ilan J

doi

10.1007/BF00356991

keywords:

subject

Has Abstract

pub_date

1975-10-01 00:00:00

pages

219-24

issue

3

eissn

0301-4851

issn

1573-4978

journal_volume

2

pub_type

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