Fractionation of nucleolar proteins by two-dimensional gel electrophoresis

Publisher Website
Google Scholar
Abstract
Isolation of nucleolar proteins from rat liver was obtained by dissociation in the presence of urea-guanidine hydrochloride, followed by high-speed centrifugation to remove nucleic acids. At least 31 fractions of nucleolar proteins were detected by isoelectrofocusing gel electrophoresis in the pH range 3.5-10. Following 2-dimensional gel electrophoresis on sodium dodecyl sulfate-polyacrylamide slab gels, more than 100 components of nucleolar proteins were identified. Of the nucleolar proteins, 2/3 were located in the pH range 5-8 following isoelectrofocusing. The molecular weights of these classes of proteins were mostly 30,000-70,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

This publication has 0 references indexed in Scilit: