Purification and partial characterization of a bovine epidermal growth factor-like polypeptide.
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.
Byatt
J C
JC
Monsanto Company, St. Louis, Missouri 63198.
Larson
B R
BR
Baganoff
M P
MP
McGrath
M F
MF
Collier
R J
RJ
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D004815:Epidermal Growth Factor / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D004847:Epithelial Cells; D007668:Kidney / Q000032:analysis*; D008321:Mammary Glands, Animal / Q000166:cytology; D051379:Mice
D000596:Amino Acids; D004815:Epidermal Growth Factor