Stability of recombinant human epidermal growth factor in various solutions.
The stability of recombinant human epidermal growth factor (hEGF) in various solutions was examined. hEGF degraded spontaneously and temperature-dependently to several degradation products in phosphate buffered saline or in 0.1 N acetic acid. The enzymatic degradation was observed in human serum or in pepsin/HCl solution. The structure and biological activities of these compounds were examined. The results suggest that the Asp11 and Trp50 residues are important for the receptor binding.
Araki
F
F
Nakamura
H
H
Nojima
N
N
Tsukumo
K
K
Sakamoto
S
S
D002851:Chromatography, High Pressure Liquid; D004355:Drug Stability; D004815:Epidermal Growth Factor / Q000032:analysis*; D006801:Humans; D011994:Recombinant Proteins / Q000032:analysis; D012996:Solutions
D011994:Recombinant Proteins; D012996:Solutions; D004815:Epidermal Growth Factor