Abstract
In the few years since the isolation of the subunit protein of microtubules (1, 2, 23, 26) work on its chemistry, localization and metabolism has proceeded at a feverish pace. In their initial studies Taylor and his co-workers noted exceptionally high levels of colchicine-binding activity in brain homogenates and in axoplasm. Weisenberg, Borisy and Taylor (31) developed a simple procedure for the purification of the microtubule subunits (tubulin) from brain enabling investigators to use large quantities of highly purified protein for biochemical studies. Studies on metabolism and distribution of tubulin in brain were aided by the observation that vinblastine quantitatively and selectively precipitated tubulin from 100,000 g supernatants of brain homogenates (17, 18, 32).
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Shelanski, M.L., Feit, H., Berry, R.W., Daniels, M.P. (1972). Some Biochemical Aspects of Neurotubule and Neurofilament Proteins. In: Davison, A.N., Mandel, P., Morgan, I.G. (eds) Functional and Structural Proteins of the Nervous System. Advances in Experimental Medicine and Biology, vol 32. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6979-0_6
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