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

Kenichi Ohtsubo, Hikoichi Sakai, Hiromu Murofushi, Ryoko Kuriyama

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


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-32P]ATP demonstrated that both subunits were phosphorylated in vitro. The incorporation of 32PO4 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 1975
Externally publishedYes


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