Abstract
A new method for isolating plant tubulin was devised. The method involves affinity chromatography with ethyl N-phenylcarbamate and Sepharose. The protein isolated by the affinity chromatography and purified by two successive chromato-graphical steps on DEAE-Sephadex A-50 and Sephadex G-200 consisted of two subunits which possessed the same mobilities as the α- and β-subunits of rabbit brain tubulin on SDS-polyacrylamide gel electrophoresis and showed colchicine-binding activity.
