Open AccessAre Cytoplasmic Microtubules Heteropolymers?
Author(s) -
Joseph Bryan,
Leslie Wilson
Publication year - 1971
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.68.8.1762
Subject(s) - microtubule , colchicine , gel electrophoresis , cytoplasm , sodium dodecyl sulfate , dimer , tubulin , amino acid , sephadex , polyacrylamide gel electrophoresis , chemistry , acrylamide , monomer , biochemistry , acetylation , urea , electrophoresis , protein subunit , biology , microbiology and biotechnology , genetics , enzyme , gene , organic chemistry , polymer
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom