Stabilization of Epidermal Growth Factor

Abstract

Human epidermal growth factor (EGF) was acylated at its three primary amine groups. The acylated derivatives were purified, characterized, and their activities and response to trypsin were compared with unmodified EGF. Modified EGF was shown to retain its biological activity but displayed a higher shelf stability and resistance to tryptic digestion in aqueous solutions as compared with the unmodified growth factor.