Autor: Thomas Nicholas Julian, Tsun Ming Chen, Amal M. Boctor, Anne B. Giordani, Galen W. Radebaugh, Scott C. Wootton, Richard I. Senderoff
Rok vydání: 1994
Předmět:
Zdroj: Pharmaceutical Research. 11:1712-1720
ISSN: 0724-8741
DOI: 10.1023/a:1018903014204
Popis: Human epidermal growth factor 1-48 (hEGF 1-48, Des(49-53)hEGF) is a single chain polypeptide (48 amino acids; 3 disulfide bonds; 5445 Da) possessing a broad spectrum of biologic activity including the stimulation of cell proliferation and tissue growth. In this study, three primary aqueous degradation products of hEGF 1-48 were isolated using isocratic, reverse phase/ion-pair HPLC. The degradation products were characterized using amino acid sequencing, electrospray ionization mass spectrometry, isoelectric focusing, and degradation kinetics. Results indicate that hEGF 1-48 degrades via oxidation (Met21), deamidation (Asn1), and succinimide formation (Asp11). The relative contribution of each degradation pathway to the overall stability of hEGF 1-48 changes as a function of solution pH and storage condition. Succinimide formation at Asp11 is favored at pH 6. The relative contribution of Met21 oxidation is increased with decreasing temperature, storage as a frozen solution (−20°C), and exposure to fluorescent light.
Databáze: OpenAIRE
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