Purification and partial characterization of a bovine epidermal growth factor-like polypeptide |
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| Authors: | J C Byatt B R Larson M P Baganoff M F McGrath R J Collier |
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| Institution: | Monsanto Company, St. Louis, Missouri 63198. |
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| Abstract: | 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. |
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