THE MECHANISM OF ACTION OF COLCHICINE: Colchicine Binding to Sea Urchin Eggs and the Mitotic Apparatus

doi:10.1083/jcb.34.2.535

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ARTICLE

THE MECHANISM OF ACTION OF COLCHICINE

: Colchicine Binding to Sea Urchin Eggs and the Mitotic Apparatus

G. G. Borisy ¹ and E. W. Taylor ¹

¹ From the Department of Biophysics, The University of Chicago, Chicago, Illinois 60637.

Dr. Borisy's present address is the MRC Laboratory of Molecular Biology, Cambridge, England

Colchicine forms a complex in vivo with a protein present infertilized or unfertilized sea urchin eggs; similar bindingwas obtained in vitro with the soluble fraction from egg homogenates.Kinetic parameters and binding equilibrium constant were essentiallythe same in vivo and in vitro. The binding site protein wasshown to have a sedimentation constant of 6S by zone centrifugation.The protein was present in extracts of the isolated mitoticapparatus at a concentration which was several times higherthan in whole-egg homogenates. It was extracted from the mitoticapparatus at low ionic strength under conditions which leadto the disappearance of microtubules. No binding could be detectedto the 27S protein, previously described by Kane, which is amajor protein component of the isolated mitotic apparatus. Theproperties of the colchicine-bindinG protein, (binding constant,sedimentation constant, Sephadex elution volume) are similarto those obtained with the protein from mammalian cells, sea-urchinsperm tails, and brain tissue, and thus support the conclusionthat the protein is a subunit of microtubules.

Submitted on January 9, 1967

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