title: Stability of recombinant human epidermal growth factor in various solutions.
abstract: 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.
authors: F
authors: F
authors: Araki
authors: H
authors: H
authors: Nakamura
authors: N
authors: N
authors: Nojima
authors: K
authors: K
authors: Tsukumo
authors: S
authors: S
authors: Sakamoto
mesh_terms: D002851:Chromatography, High Pressure Liquid; D004355:Drug Stability; D004815:Epidermal Growth Factor / Q000032:analysis*; D006801:Humans; D011994:Recombinant Proteins / Q000032:analysis; D012996:Solutions
chemical_list: D011994:Recombinant Proteins; D012996:Solutions; D004815:Epidermal Growth Factor