Fractionation of nucleolar proteins by two-dimensional gel electrphoresis.
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.
D000818:Animals; D002466:Cell Nucleolus / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D009698:Nucleoproteins / Q000302:isolation & purification; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D051381:Rats
D046911:Macromolecular Substances; D009698:Nucleoproteins; D010446:Peptide Fragments