Tryptic peptide mapping of core polypeptide from heterogeneous ribonucleoprotein particles.
The core proteins of heterogeneous ribonucleoprotein particles, which migrate as four major bands on one-dimensional sodium dodecyl sulphate-polyacrylamide gels, exhibit an complex pattern on two-dimensional gels in which each protein resolves into strings of polypeptides of differing charge. Tryptic peptide mapping was employed to analyse the structural relationship of their components. The 34,000-dalton protein (polypeptide-group B) resolves into a string of seven major components, of which four have been analysed. Tryptic peptide maps indicated that minor variants of at least two proteins occur in this group. The A group of polypeptides, comprising six major components of mol.wt. 32,000 and the D group, comprising three major polypeptides of mol.wt. 40,000, were also examined. Tryptic peptide maps indicate that the two protein types are fundamentally different from each other and from the B-group proteins, but they again exhibit minor variation consistent with post-translational modification.
D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009698:Nucleoproteins / Q000032:analysis*; D010455:Peptides / Q000032:analysis*; D014176:Protein Biosynthesis; D012332:RNA, Heterogeneous Nuclear; D012261:Ribonucleoproteins / Q000032:analysis*; D014357:Trypsin
D009698:Nucleoproteins; D010455:Peptides; D012332:RNA, Heterogeneous Nuclear; D012261:Ribonucleoproteins; D014357:Trypsin