Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

Tubulin dimers isolated from brain contain two GTP binding sites, a nonexchangeable site and an exchangeable site. To localize the exchangeable site, we used a photoaffinity analog of GTP, 8-azidoguanosine triphosphate (8-N3GTP), which supports tubulin polymerization in the absence of activating light. Photolysis of tubulin polymerized in the presence of 0.01 to 0.1 mM [beta, gamma-32P]8-N3GTP resulted in covalent incorporation of radioactivity only onto the beta monomer. Photolysis with 8-N3GTP also prevented any further repolymerization of the tubulin whereas like treatment in the presence of GTP had no effect. Preincubation of tubulin with GTP prevented photo-incorporation of [beta, gamma-32P]8-N3GTP whereas preincubation with ATP did not.

Bibliography

Geahlen, R. L., & Haley, B. E. (1977). Interactions of a photoaffinity analog of GTP with the proteins of microtubules. Proceedings of the National Academy of Sciences, 74(10), 4375–4377.

Authors 2
  1. R L Geahlen (first)
  2. B E Haley (additional)
References 0 Referenced 44

None

Dates
Type When
Created 19 years, 2 months ago (May 31, 2006, 3:23 a.m.)
Deposited 3 years, 4 months ago (April 13, 2022, 11 a.m.)
Indexed 1 year, 1 month ago (July 2, 2024, 11:16 a.m.)
Issued 47 years, 10 months ago (Oct. 1, 1977)
Published 47 years, 10 months ago (Oct. 1, 1977)
Published Online 47 years, 10 months ago (Oct. 1, 1977)
Published Print 47 years, 10 months ago (Oct. 1, 1977)
Funders 0

None

@article{Geahlen_1977, title={Interactions of a photoaffinity analog of GTP with the proteins of microtubules.}, volume={74}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.74.10.4375}, DOI={10.1073/pnas.74.10.4375}, number={10}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Geahlen, R L and Haley, B E}, year={1977}, month=oct, pages={4375–4377} }