## Abstract Tubulin is an attractive and established target for anticancer therapy. To date, the only method to determine the binding of inhibitor to tubulin has been competitive radioligand binding assays. We developed a nonβradioactive mass spectrometry (MS) binding assay to study the tubulin bin
A new colchicine binding assay for tubulin
β Scribed by Peter Sherline; Cynthia K. Bodwin; David M. Kipnis
- Publisher
- Elsevier Science
- Year
- 1974
- Tongue
- English
- Weight
- 415 KB
- Volume
- 62
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
A simple and sensitive procedure is described for assaying tubulin. the subunit protein of microtubules. Tubulin is equilibrated with ['Hlcolchicine after which the remaining free colchicine is removed by adsorption to activated charcoal. Values for the amount of tubulin in various rat tissues have been determined by both the charcoal method and by gel filtration on Sephadex G-100, and in all cases the values determined by the two methods correspond closely.
π SIMILAR VOLUMES
A standardized assay method has been developed for assessing the binding capacity of derivitized concanavalin A (con A). The method takes advantage of the fact that concanavalin A binds to Sephadex G-75 in an cr-methyt-rr-mannopyranoside-inhibitable manner. Using this binding assay we have found tha