Complete amino acid sequence of beta-tubulin from porcine brain.
- 1 July 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (7), 4156-4160
- https://doi.org/10.1073/pnas.78.7.4156
Abstract
The primary structure of porcine brain .beta.-tubulin was determined by automated and manual Edman degradation of 6 sets of overlapping peptides. The protein consists of 445 amino acid residues and has a minimum of 6 positions that are heterogeneous, indicating at least 2 .beta.-tubulin 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.This publication has 31 references indexed in Scilit:
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