Beta-epidermal growth factor is the des-asparaginyl form of the polypeptide.
Reversed-phase high performance liquid chromatography of mouse epidermal growth factor (EGF) yielded two major forms, alpha- and beta-EGF, and a minor component, gamma-EGF. All three forms exhibited receptor-binding activity. Analysis of native alpha- and beta-EGF by mass spectrometry and partial Edman degradation led us to propose that alpha-EGF has a primary structure equivalent to that originally reported for EGF and that beta-EGF is the des-asparaginyl form of the polypeptide. When the purified alpha- and beta-polypeptides were cultured with human embryonic palatal mesenchymal cells stimulation of cell proliferation was observed at concentrations as low as 0.01 ng/ml with maximal stimulation occurring at about 1 ng/ml. Essentially no difference was noted in the mitogenic potency of the two forms. This suggests that the NH2-terminal region of EGF is not critical for mitogenic activity.
DiAugustine
R P
RP
Walker
M P
MP
Klapper
D G
DG
Grove
R I
RI
Willis
W D
WD
Harvan
D J
DJ
Hernandez
O
O
D000595:Amino Acid Sequence; D001216:Asparagine; D002455:Cell Division / Q000187:drug effects; D002851:Chromatography, High Pressure Liquid; D004815:Epidermal Growth Factor / Q000032:analysis*; D066246:ErbB Receptors; D006801:Humans; D013058:Mass Spectrometry; D011956:Receptors, Cell Surface / Q000378:metabolism; D013329:Structure-Activity Relationship
D011956:Receptors, Cell Surface; D004815:Epidermal Growth Factor; D001216:Asparagine; D066246:ErbB Receptors