Two-dimensional gel electrophoresis of myc gene products after cleavage by viral protease p15.
An analysis of myc-specific protein (p58myc), precipitated from cells transformed by virus OK10, by means of two-dimensional gel electrophoresis revealed the presence of two variants of p58myc differing in their isoelectric point. Both variants are completely cleaved by protease p15 as is the c-myc gene product precipitated from 16Q cells. The cleavage fragments of c-myc and v-myc protein do not differ in size but differ in their stability.
D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002460:Cell Line; D003370:Coturnix; D004591:Electrophoresis, Polyacrylamide Gel; D009857:Oncogenes; D010447:Peptide Hydrolases / Q000378:metabolism*; D014764:Viral Proteins / Q000032:analysis*
D014764:Viral Proteins; D010447:Peptide Hydrolases; D016282:Aspartic Acid Endopeptidases; C036946:protease p15