Abstract
The NS protein of vesicular stomatitis virus is the only phosphorylated nucleocapsid protein. The amount of NS phosphorylation appears to regulate the activity of the protein in the transcription of the virus genome. Several methods have been used to separate NS subspecies containing different amounts of phosphate, but the relationships among the subspecies separated by different workers have been unclear. We report that the isoelectric points of NS molecules were abnormally acidic in some commercial ampholytes, but favorable ampholytes resolved multiple phosphorylated NS subspecies with isoelectric points ranging from pH 6.8 to 7.2. The most highly phosphorylated NS molecules had more acidic isoelectric points, and they exhibited greater electrophoretic mobilities in two previously employed electrophoretic systems.