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Title: Complete amino acid sequence of beta-tubulin from porcine brain. Author: Krauhs E, Little M, Kempf T, Hofer-Warbinek R, Ade W, Ponstingl H. Journal: Proc Natl Acad Sci U S A; 1981 Jul; 78(7):4156-60. PubMed ID: 6945576. 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.[Abstract] [Full Text] [Related] [New Search]