猪脑α-微管蛋白的完整氨基酸序列
Complete amino acid sequence of alpha-tubulin from porcine brain.
作者信息
Ponstingl H, Krauhs E, Little M, Kempf T
出版信息
Proc Natl Acad Sci U S A. 1981 May;78(5):2757-61. doi: 10.1073/pnas.78.5.2757.
Abstract
The amino acid sequence of alpha-tubulin from porcine brain was determined by automated and manual Edman degradation of eight sets of overlapping peptides. It comprises 450 residues plus a COOH-terminal tyrosine that is present only in 15% of the material. A region of 40 residues at the COOH-terminus is highly acidic, mainly due to 16 glutamyl residues. This high concentration of negative charge suggests a region for binding cations. At least six positions, most of them around position 270, are occupied by two amino acid residues each. Several of these exchange sites were assigned to specific peptides by analysis of the purified corresponding fragments. These data indicate four alpha-tubulins in porcine brain. Although alpha-tubulin on the whole is unrelated to other proteins, there are regions that can be correlated to sequences of the myosin head, to actin, to tropomyosin, and to troponins C and T.
摘要
通过对八组重叠肽段进行自动和手动的埃德曼降解法，测定了猪脑α-微管蛋白的氨基酸序列。它由450个残基加上一个仅存在于15%的材料中的COOH末端酪氨酸组成。COOH末端的40个残基区域高度酸性，主要是由于16个谷氨酰残基。这种高浓度的负电荷表明存在一个结合阳离子的区域。至少有六个位置，其中大部分在270位左右，每个位置被两个氨基酸残基占据。通过对纯化的相应片段进行分析，将其中几个交换位点指定给特定的肽段。这些数据表明猪脑中存在四种α-微管蛋白。虽然α-微管蛋白总体上与其他蛋白质无关，但存在一些区域可与肌球蛋白头部、肌动蛋白、原肌球蛋白以及肌钙蛋白C和T的序列相关联。
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