Structural relationship of the heterogeneous nuclear ribonucleoprotein core polypeptides from rat liver nuclei

The individual species of the core polypeptide family of 30-50 S hnRNP resolved on two-dimensional electrophoresis (nonequilibrium pH gradient gels combined with sodium dodecyl sulfate polyacrylamide gels) have been subjected to the enzymatic cleavage procedure of D.W. Cleveland, S.G. Fischer, M.W. Kirschner, and U.K. Laemmli (1977, J. Biol. Chem. 252, 1102-1106). This allowed direct and extensive structural analysis of almost every member of the core polypeptide family by comparison of their overall peptide maps. Thus, the over 20 protein species, resolved on two-dimensional gels, from the four major bands (A, B, C, and D) on one-dimensional sodium dodecyl sulfate-polyacrylamide gels, belong mainly to three distinct protein groups, and each species represents the product of extensive post-translational modification. Furthermore, their inability to bind the lectin concanavalin A makes it unlikely that the modifications of these proteins represent glycosylations. Therefore, the core polypeptides cannot be glycoproteins of the general class with affinity for concanavalin A.