Characterization of the phosphorylated small enzyme subunit, NS, of the vesicular stomatitis virus RNA polymerase.
NS protein of vesicular stomatitis virus was shown to migrate with a mobility consistent with the molecular weight predicted from the published cDNA sequence on polyacrylamide gels containing the detergent cetyltrimethylammonium bromide at low pH. Cyanogen bromide cleavage of NS protein produced a large acidic amino-terminal peptide, as predicted by the sequence, which contained the majority of the phosphate residues. However, analysis of tryptic peptides by high-performance liquid chromatography suggested that there may be inaccuracies in the sequence of the carboxyl terminus of the sequence.
D000469:Alkaline Phosphatase; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D012321:DNA-Directed RNA Polymerases / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells / Q000201:enzymology; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation; D014357:Trypsin; D014721:Vesicular stomatitis Indiana virus / Q000201:enzymology*; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins / Q000302:isolation & purification*
D046911:Macromolecular Substances; D010446:Peptide Fragments; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins; D012321:DNA-Directed RNA Polymerases; D000469:Alkaline Phosphatase; D014357:Trypsin