Purification and partial characterization of a bovine epidermal growth factor-like polupeptide

J. C. Byatt, B. R. Larson, M. P. Baganoff, M. F. McGrath, R. J. Collier

Research output: Contribution to journalArticle

5 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1179-1187
Number of pages9
JournalBiochemistry International
Volume20
Issue number6
StatePublished - Jun 12 1990

ASJC Scopus subject areas

  • Biochemistry

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