Stabilization of hepatic colchicine-binding activity by organic acids

R. B. Jennett, D. J. Tuma, W. T. Sorrell, M. F. Sorrell

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Previous work has shown that the total hepatic tubulin pool and the hepatic microtubule-derived tubulin pool do not have identical [3H]colchicine binding properties. Rapid loss of colchicine-binding activity was noted in the microtubule-derived fractions of liver tubulin. Furthermore, quantitative determination of the total and polymerized tubulin in the liver by the [3H]colchicine-binding assay was hampered by rapid and unequal loss of binding sites under assay conditions. The organic acids, glutamate and glucose 1-phosphate, have been shown to stabilize calf brain tubulin against loss of colchicine-binding sites. Therefore, these compounds were tested as possible protecting agents against loss of colchicine binding activity of liver tubulin. It was found that these agents stabilized liver tubulin under [3H]colchicine-binding conditions. Additional experiments showed that these agents also prevented the rapid loss of colchicine-binding activity that occurred when purified brain tubulin was exposed to liver supernates. These results suggest that the inclusion of the organic acids, glutamate and glucose 1-phosphate, may modify the time decay properties of liver tubulin in solution. Further, these data suggest that these protecting agents may be of analytical value in [3H]colchicine-binding assay systems for liver tubulin.

Original languageEnglish (US)
Pages (from-to)304-310
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - Jan 1985

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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