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The analysis of the proteins of heterogeneous ribonucleoprotein particles on two‐dimensional polyacrylamide gels
Author(s) -
Wilks Andrew F.,
Knowler John T.
Publication year - 1980
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150010306
Subject(s) - ribonucleoprotein , isoelectric focusing , fractionation , chemistry , electrophoresis , polyacrylamide gel electrophoresis , heterogeneous nuclear ribonucleoprotein , polyacrylamide , chromatography , isoelectric point , biophysics , biochemistry , biology , rna , polymer chemistry , gene , enzyme
Methods of two‐dimensional protein fractionation have been analysed for their suitability for the analysis of heterogeneous ribonucleoprotein (hnRNP) particles. Nonequilibrium pH gradient electrophoresis gives the best overall fractionation and reveals that the dominant “core” proteins possess charge heterogeneity. For the analysis of the minor components of the particles, it may be preferable to overload isoelectric focusing gels and allow the basic core proteins, which comprise 70% of the total protein, to migrate off the gel. This does, however, result in the loss of some basic minor polypeptides.