Binding of colchicine to renal tubulin at 5°C

Larry D. Barnes, Angela K. Robinson, Robert F. Williams, Paul M. Horowitz

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Previous reports in the literature state that the binding of colchicine to soluble tubulin is negligible at 0 - 4°C as measured by non-equilibrium binding methods. In contrast, we have detected significant binding of colchicine to tubulin at 5°C. Furthermore, for the first time equilibrium dialysis has been used to measure colchicine binding. The value of the dissociation constant was 1.8 μM at 5°C, and the stoichiometry of colchicine binding at 5°C equaled that at 37°C. Dissociation at 5°C of bound colchicine was negligible over a period of 23 h, and the estimated minimal half-time of dissociation was 150 h.

Original languageEnglish (US)
Pages (from-to)866-872
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Nov 15 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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