Electrophoretic separation of tubulin alpha and beta subunits after S-sulfonation.
The modification of tubulin cystine and cystine residues to S-sulfocysteines caused a distinct separation of the alpha and beta subunits in a continuous sodium dodecyl sulfate polyacrylamide gel system. The well-separated subunit bands permitted investigation of the phosphorylation of alpha and beta tubulin subunits. The incubation of tubulin fraction with [gamma-32P]ATP demonstrated that both subunits were phosphorylated in vitro. The incorporation of 32-PO4 into sea urchin eggs, however, failed to cause phosphorylation of tubulin in vivo.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D003545:Cysteine / Q000032:analysis; D003553:Cystine / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D046911:Macromolecular Substances; D008970:Molecular Weight; D009419:Nerve Tissue Proteins; D010063:Ovum / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D012617:Sea Urchins / Q000032:analysis; D013451:Sulfonic Acids; D014404:Tubulin / Q000378:metabolism
D046911:Macromolecular Substances; D009419:Nerve Tissue Proteins; D013451:Sulfonic Acids; D014404:Tubulin; D003553:Cystine; D000255:Adenosine Triphosphate; D003545:Cysteine