Electrophoretic separation of tubulin α and β subunits after S-sulfonation

Kenichi Ohtsubo, Hikoichi Sakai, Hiromu Murofushi, Ryoko Kuriyama

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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 languageEnglish (US)
Pages (from-to)17-21
Number of pages5
JournalJournal of Biochemistry
Issue number1
StatePublished - Jan 1 1975


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