Stabilization of the colchicine-binding activity of tubulin by glutathione and by dietary selenium-deficiency.
The lability of tubulin in supernatant fluids from rat brain was studied by measuring the loss of colchicine-binding activity. During incubation at 37 degrees C for 1 hr approximately 50% of the binding activity of rat brain supernatant fluids was lost. This loss was reduced by mercaptoethanol or reduced glutathione. Anaerobic conditions did not affect loss of binding, while oxygen markedly reduced it, especially in the presence of reduced glutathione. Supernatant fluids prepared from brains of animals deficient in selenium showed a lower loss of binding than those from selenium-supplemented controls.
D000818:Animals; D001921:Brain / Q000378:metabolism*; D003078:Colchicine / Q000378:metabolism*; D004355:Drug Stability; D005978:Glutathione / Q000494:pharmacology*; D008623:Mercaptoethanol / Q000494:pharmacology; D010100:Oxygen; D011485:Protein Binding / Q000187:drug effects; D051381:Rats; D012643:Selenium / Q000172:deficiency*; D014404:Tubulin / Q000378:metabolism*
D014404:Tubulin; D008623:Mercaptoethanol; D005978:Glutathione; D012643:Selenium; D010100:Oxygen; D003078:Colchicine