一种牛表皮生长因子样多肽的纯化及部分特性鉴定
Purification and partial characterization of a bovine epidermal growth factor-like polypeptide.
作者信息
Byatt J C, Larson B R, Baganoff M P, McGrath M F, Collier R J
机构信息
Monsanto Company, St. Louis, Missouri 63198.
出版信息
Biochem Int. 1990;20(6):1179-87.
A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.
开发了一种异源放射受体测定法来追踪从牛肾中纯化一种表皮生长因子（EGF）样多肽的过程。使用一种新型亲和柱（固定有附着在葡聚糖凝胶珠上的A431细胞）促进了生长因子的纯化。根据氨基酸组成估计纯化的EGF-LP的分子量为5480。纯化的EGF样多肽刺激了牛乳腺上皮细胞的增殖，并且似乎与小鼠EGF具有同等效力。现有证据表明，纯化的分子与牛转化生长因子-α（TGF-α）不同。
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