| Literature DB >> 2787214 |
F Araki, H Nakamura, N Nojima, K Tsukumo, S Sakamoto.
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.Entities:
Mesh:
Substances:
Year: 1989 PMID: 2787214 DOI: 10.1248/cpb.37.404
Source DB: PubMed Journal: Chem Pharm Bull (Tokyo) ISSN: 0009-2363 Impact factor: 1.645