COMPLETE AMINO-ACID-SEQUENCE OF BETA-TUBULIN FROM PORCINE BRAIN
COMPLETE AMINO-ACID-SEQUENCE OF BETA-TUBULIN FROM PORCINE BRAIN
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DOI：
10.1073/pnas.78.7.4156
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发表时间：
1981-01-01
期刊：
影响因子：
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通讯作者：
PONSTINGL, H
中科院分区：
文献类型：
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作者：
KRAUHS, E;LITTLE, M;PONSTINGL, H
猪脑β的一级结构-通过自动和手动Edman降解6组重叠肽测定微管蛋白。该蛋白质由445个氨基酸残基组成，并且具有最少6个异质的位置，表明至少2 β-猪脑微管蛋白。比较α-β的最佳比对序列微管蛋白和β-微管蛋白表明它们的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NH 2-末端。
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.