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. 1971 Aug;68(8):1762–1766. doi: 10.1073/pnas.68.8.1762

Are Cytoplasmic Microtubules Heteropolymers?

Joseph Bryan *,*, Leslie Wilson †,†
PMCID: PMC389288  PMID: 5288762

Abstract

Colchicine-binding protein, considered to be microtubule protein, was purified from chick embryo brain by column chromatography in one step on DEAE-Sephadex. The active colchicine-binding unit is a dimer, MW 115,000 ± 5000, which is composed of two nonidentical monomeric units. The two subunits are separable by urea-acrylamide gel electrophoresis after they have been reduced and acetylated. Sodium dodecyl sulfate-acrylamide gel electrophoresis indicates that the subunits both have molecular weights of 55,000 ± 2000. The amino-acid compositions of the two subunits showed statistically significant differences in six amino-acid residues. These results indicate that colchicine-sensitive cytoplasmic microtubules are heteropolymers.

Keywords: chick embryo brain, subunits, amino-acid composition

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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