Abstract
The primary structure of porcine brain beta-tubulin was determined by automated and manual Edman degradation of six sets of overlapping peptides. The protein consists of 445 amino acid residues and has a minimum of six positions that are heterogeneous, indicating at least two beta-tubulins in porcine brain. Comparison of the optimally aligned sequences of alpha-tubulin and beta-tubulin indicates that 41% of their primary structures are identical. A region rich in glycyl residues is similar both in sequence and predicted secondary structure to the phosphate binding loop of several nucleotide binding enzymes. beta-Tubulin contains a highly acidic COOH-terminal region that resembles the NH2-terminus of troponin T.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 4:44 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 11:38 a.m.) |
Indexed | 3 weeks, 4 days ago (Aug. 2, 2025, 1:26 a.m.) |
Issued | 44 years, 1 month ago (July 1, 1981) |
Published | 44 years, 1 month ago (July 1, 1981) |
Published Online | 44 years, 1 month ago (July 1, 1981) |
Published Print | 44 years, 1 month ago (July 1, 1981) |
@article{Krauhs_1981, title={Complete amino acid sequence of beta-tubulin from porcine brain.}, volume={78}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.78.7.4156}, DOI={10.1073/pnas.78.7.4156}, number={7}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Krauhs, E and Little, M and Kempf, T and Hofer-Warbinek, R and Ade, W and Ponstingl, H}, year={1981}, month=jul, pages={4156–4160} }