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Stability of recombinant human epidermal growth factor in various solutions.

作者信息

Araki F, Nakamura H, Nojima N, Tsukumo K, Sakamoto S

出版信息

Chem Pharm Bull (Tokyo). 1989 Feb;37(2):404-6. doi: 10.1248/cpb.37.404.

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.

摘要

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