Higashi K, Ishibashi S
Biochem Biophys Res Commun. 1985 Oct 15;132(1):193-7. doi: 10.1016/0006-291x(85)91006-x.
A protein was isolated from the soluble fraction of rat brain by affinity chromatography with Sepharose to which guanine nucleotide-binding inhibitory regulatory protein in adenylate cyclase system, Ni, was immobilized. The molecular weight of this protein, specifically bound to the Ni-affinity column, was estimated as 54,000 on sodium dodecylsulfate-polyacrylamide gel electrophoresis. Alternately prepared tubulin also bound to the Ni-affinity column. The amino acid compositions of these proteins were also identical. It is strongly suggested that this Ni-binding cytosolic protein is tubulin.
通过与固定有腺苷酸环化酶系统中鸟嘌呤核苷酸结合抑制调节蛋白Ni的琼脂糖进行亲和层析,从大鼠脑的可溶部分分离出一种蛋白质。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上,与Ni亲和柱特异性结合的这种蛋白质的分子量估计为54,000。交替制备的微管蛋白也与Ni亲和柱结合。这些蛋白质的氨基酸组成也相同。强烈提示这种与Ni结合的胞质蛋白是微管蛋白。