The modification of tubulin cysteine and cystine residues to S-sulfocysteines caused a distinct separation of the α and β subunits in a continuous sodium dodecyl sulfate polyacrylamide gel system. The well-separated subunit bands permitted investigation of the phosphorylation of α and β tubulin subunits. The incubation of tubulin fraction with [γ -32 P]ATP demonstrated that both subunits were phosphorylated in vitro. The incorporation of 32 PO 4 into sea urchin eggs, however, failed to cause phosphorylation of tubulin in vivo.
|Original language||English (US)|
|Number of pages||5|
|Journal||Journal of Biochemistry|
|State||Published - Jan 1 1975|