Tubulin: An Integral Protein of Mammalian Synaptic Vesicle Membranes
Version of Record online: 5 OCT 2006
Journal of Neurochemistry
Volume 34, Issue 1, pages 26–32, January 1980
How to Cite
Zisapel, N., Levi, M. and Gozes, I. (1980), Tubulin: An Integral Protein of Mammalian Synaptic Vesicle Membranes. Journal of Neurochemistry, 34: 26–32. doi: 10.1111/j.1471-4159.1980.tb04617.x
- Issue online: 5 OCT 2006
- Version of Record online: 5 OCT 2006
- Received April 4, 1979; revised June 11, 1979; accepted June 22, 1979.
Abstract: The major protein in isolated synaptic vesicles from bovine cerebral cortex has been compared to tubulin by sodium dodecyl sulphate-urea polyacrylamide gel electrophoresis, by two-dimensional gel electrophoresis and by peptide mapping following limited proteolysis of the protein by Staphylococcus aureus protease. The results establish in purified synaptic vesicles the presence of tubulin, which is composed of the α and β subunits. In the presence of ethyleneglycolbis (aminoethyl ether)-N, N'-tetraacetic acid (EGTA) or magnesium in the isolation buffers, the synaptic vesicles contained mainly the α-tubulin whereas the β subunit was less abundant. Similarly, synaptosomal plasma membranes that were prepared in the presence of EGTA also contained more of α-tubulin than of the β subunit. Non-ionic detergents such as Triton X-100 or Nonidet P-40 failed to solubilize the tubulin from the synaptic vesicles. Ionic detergents such as deoxycholate and sodium dodecyl sulphate solubilized all the vesicle proteins, including tubulin. The results indicate that α-tubulin is an integral vesicle membrane protein, whereas most of the β sub-unit is peripherally attached and can be easily dissociated from the vesicle membrane with EGTA.