In vitro formation of different tubulin polymers from purified tubulin of Ehrlich ascites tumor cells
- 24 January 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 151 (2) , 286-290
- https://doi.org/10.1016/0014-5793(83)80088-x
Abstract
Preparations of cycled tubulin from Ehrlich ascites tumor cells contain several acessory proteins; once or twice cycled microtubule preparations are usually composed of fibers 10 nm in diameter, but lack vimentin. Highly purified tubulin consists of α- and β-tubulin and a minor component which was identified by peptide mapping as a second β-chain. This pure tubulin is able to form in vitro at low concentrations (1 mg protein/ml) fibers of about 10 nm width, and at higher concentrations (3.5 mg protein/ml) normal microtubules.Keywords
This publication has 17 references indexed in Scilit:
- THE STRUCTURE OF MICROTUBULES*Annals of the New York Academy of Sciences, 1982
- Chapter 3 Assembly-Disassembly Purification and Characterization of Microtubule Protein without GlycerolPublished by Elsevier ,1982
- Properties of a Ca2+‐Activated Protease Specific for the Intermediate‐Sized Filament Protein Vimentin in Ehrlich‐Ascites‐Tumour CellsEuropean Journal of Biochemistry, 1981
- Identification of a second β chain in pig brain tubulinFEBS Letters, 1979
- Assembly of nonneural microtubules in the absence of glycerol and microtubule-associated proteinsBiochemistry, 1979
- In vitro reconstitution of calf brain microtubules: effects of macromoleculesBiochemistry, 1978
- In vitro assembly of tubulin from nonneural cells (Ehrlich ascites tumor cells)Biochemistry, 1977
- Identity and polymerization-stimulatory activity of the nontubulin proteins associated with microtubulesBiochemistry, 1977
- In vitro assembly of pure tubulin into microtubules in the absence of microtubule-associated proteins and glycerol.Proceedings of the National Academy of Sciences, 1977
- Microtubule-associated proteins and the stimulation of tubulin assembly in vitroBiochemistry, 1976