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PMID: 5288762 Published · ppublish English Journal Article

Are cytoplasmic microtubules heteropolymers?

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 68 ·No. 8 ·1971-08-00 ·Pages 1762-6

Bryan J, Wilson L

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.

MeSH Terms
Amino Acids/analysis Animals Autoradiography Brain Chemistry Chick Embryo Chromatography, Ion Exchange Colchicine Densitometry Electrophoresis Microtubules/analysis Molecular Weight Nerve Tissue Proteins/analysis,isolation & purification Polymers/analysis Protein Binding Tritium
Chemicals
Amino Acids Nerve Tissue Proteins Polymers Tritium Colchicine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bryan J
Wilson L
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24 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.68.8.1762
Published
1971-08-00
Pages
1762-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC389288
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.68.8.1762 PMC Full Text View journal details
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