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The comparison of rat liver rough endoplasmic reticulum membrane proteins before and afterin vitroremoval of its bound ribosomes

✍ Scribed by Henryk H. Czosnek; Nathan Groot; Abraham A. Hochberg

Publisher: Springer
Year: 1975
Tongue: English
Weight: 982 KB
Volume: 2
Category: Article
ISSN: 0301-4851
DOI: 10.1007/bf00357541

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✦ Synopsis

The comparison of the proteins of rat liver rough membrane after strippirig with EDTA or KCl-puromycin by two dimensional gel electrophoresis is described. By stripping the membrane with EDTA, most of the basic ribosomal proteins are still attached to the membrane; in contrast to the EDTA stripping method, treatment with KCl-puromycin removes most of the ribosomal proteins and does not remove any of the membranal proteins.

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Ribosomal proteins from pure free and membrane-bound rat liver polysomes were analyzed with a highly resolutive two-dimensional gel electrophoresis technique, using sodium dodecyl sulfate in the second dimension. Three acidic proteins found in free polysomes were always absent from the membrane-boun