PMID: 3272Jan 1, 1976

Fractionation of nucleolar proteins by two-dimensional gel electrphoresis

Canadian Journal of Biochemistry
G JackowskiC C Liew


Isolation of nucleolar proteins 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 pH range 3.5-10. Following two-dimensional gel electrophoresis on sodium dodecyl sulfate-polyacrylamide slab gels, more than 100 components of nucleolar proteins were identifieid. Two-thirds of nucleolar proteins were located in the pH range 5-8 following isoelectrofocusing. The molecular weights of these classes of proteins were shown to be mostly 30000-70000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.


Feb 15, 1980·Experientia·H KlingG Sawatzki
Jul 1, 1979·Journal of the Neurological Sciences·I H FraserC C Liew
Jun 1, 1981·Journal of the Neurological Sciences·S OkuC C Liew
Jul 1, 1983·Journal of the Neurological Sciences·S OkuB A Britt
Oct 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·C C Liew, P K Chan

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