Abstract
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) |
---|---|
Pages (from-to) | 17-21 |
Number of pages | 5 |
Journal | Journal of Biochemistry |
Volume | 77 |
Issue number | 1 |
State | Published - Jan 1 1975 |