The assembly of tubulin into membranes

Howard Feit, Jerry W. Shay

Research output: Contribution to journalArticle

15 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)324-331
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume94
Issue number1
DOIs
StatePublished - May 14 1980

Fingerprint

Tubulin
Membranes
Maytansine
Microtubule-Associated Proteins
Electrophoresis, Gel, Two-Dimensional
Colchicine
Electrophoresis
Microtubules
Polymerization
Brain
Phospholipids
Gels
Temperature

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The assembly of tubulin into membranes. / Feit, Howard; Shay, Jerry W.

In: Biochemical and Biophysical Research Communications, Vol. 94, No. 1, 14.05.1980, p. 324-331.

Research output: Contribution to journalArticle

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