PMID: 427627Jan 1, 1979

Characterization of proteins associated with nuclear ribonucleoprotein particles by two-dimensional polyacrylamide gel electrophoresis

Canadian Journal of Biochemistry
D Suria, C C Liew


Rat liver nuclear ribonucleoprotein particles were prepared by two different methods and defined as 40S ribonucleoprotein (40S RNP) and heterogeneous nuclear ribonucleoprotein (HnRNP) particles. The RNP particles were either solubilized in 8 M urea--6 mM 2-mercaptoethanol--20 mM glycine--20 mM Tris--HCl (pH 8.4) or subjected to removal of RNA by phenol extraction prior to solubilizing the proteins in the urea buffer. The proteins associated with 40S RNP and HnRNP were heterogeneous and very similar in their electrophoretic patterns when analyzed by two-dimensional PAGE, except a protein with molecular weight of 62 000 and an isoelectric point (pI) of 6.2 was present only in HnRNP particles. At least 12 major and 22 minor components could be identified in both preparations. The major proteins were found at pI values varying from 6.0 to 8.5 and with molecular weights from 32 000 to 42 000, and a group of proteins with molecular weight approximately 65 000 were more prominent in HnRNP than in 40S RNP. The other components were found mainly at pI ranges from 5.0 to 6.5 with molecular weights from 43 000 to 65 000. The phenol method extracted essentially all proteins associated with either 40S RNP and HnRNP, but was less effective i...Continue Reading


Apr 21, 1993·Molecular and Cellular Biochemistry·C C Liew, E Cukerman
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, 1980·The Journal of Cell Biology·K E Peters, D E Commings
May 24, 1980·Nucleic Acids Research·S MuyldermansR Hamers
Jan 2, 1985·European Journal of Biochemistry·H E WilkK P Schäfer
Sep 13, 1983·Biochemistry·H E WilkK P Schäfer

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