The assembly of tubulin into membranes

Howard Feit; Jerry W. Shay

doi:10.1016/S0006-291X(80)80224-5

The assembly of tubulin into membranes

Howard Feit, Jerry W. Shay

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

Tubulin in high-speed supernatants of brain undergoes an alternate form of polymerization into structures that resemble membranes rather than microtubules. The reaction required elevated temperature (37°C) and was prevented by 1mM CaCl₂ or 10^-4 M maytansine. The membraneous material was composed of tubulin (80%) and microtubule-associated proteins (8%) and contained phospholipids. The tubulin was identified on the basis of comigration in two-dimensional gel electrophoresis and colchicine-binding activity.

Original language	English (US)
Pages (from-to)	324-331
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	94
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(80)80224-5
State	Published - May 14 1980

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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The assembly of tubulin into membranes

Abstract

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