Krauhs E, Little M, Kempf T, Hofer-Warbinek R, Ade W, Ponstingl H
Proc Natl Acad Sci U S A. 1981 Jul;78(7):4156-60. doi: 10.1073/pnas.78.7.4156.
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.
通过对六组重叠肽进行自动和手动的埃德曼降解，确定了猪脑β-微管蛋白的一级结构。该蛋白质由445个氨基酸残基组成，至少有六个位置存在异质性，表明猪脑中至少有两种β-微管蛋白。α-微管蛋白和β-微管蛋白的最佳比对序列比较表明，它们41%的一级结构是相同的。富含甘氨酰残基的区域在序列和预测的二级结构上均与几种核苷酸结合酶的磷酸结合环相似。β-微管蛋白含有一个高度酸性的COOH末端区域，类似于肌钙蛋白T的NH2末端。
