Singhofer-Wowra M, Clayton L, Dawson P, Gull K, Little M
Eur J Biochem. 1986 Dec 15;161(3):669-79. doi: 10.1111/j.1432-1033.1986.tb10492.x.
Starting with 7.7 mg of a beta-tubulin isolated from myxamoebae of the slime mould Physarum polycephalum, 90% of the sequence has been determined by the Edman degradation of peptides generated by cyanogen bromide, trypsin and Staphylococcus aureus protease. Differences to other beta-tubulins are mainly conservative and spread evenly throughout the chain except for a high concentration at the C-terminus. The Physarum beta-tubulin shows most homology to Chlamydomonas beta-tubulin (90.5%) and least homology to yeast beta-tubulin (S. cerevisiae, 73.4%). Two tryptic peptides were isolated in approximately equal quantities which were identical except in one position (S/ALTVPELTQRMFDA) showing that at least two beta-tubulins are present in myxamoebae. However, since this was the only heterogeneity found, these beta-tubulins are probably very similar.
从7.7毫克从多头绒泡菌的变形体中分离出的β-微管蛋白开始，通过对溴化氰、胰蛋白酶和金黄色葡萄球菌蛋白酶产生的肽段进行埃德曼降解，已确定了90%的序列。与其他β-微管蛋白的差异主要是保守的，除了在C端有高浓度外，在整个链中分布均匀。多头绒泡菌的β-微管蛋白与衣藻β-微管蛋白的同源性最高（90.5%），与酵母β-微管蛋白（酿酒酵母，73.4%）的同源性最低。分离出了两个数量大致相等的胰蛋白酶肽段，它们除了一个位置（S/ALTVPELTQRMFDA）不同外完全相同，这表明变形体中至少存在两种β-微管蛋白。然而，由于这是唯一发现的异质性，这些β-微管蛋白可能非常相似。
