Home LiteratureArticle Details
PMID: 2787214 Published · ppublish English Journal Article

Stability of recombinant human epidermal growth factor in various solutions.

Chemical & pharmaceutical bulletin ·Vol. 37 ·No. 2 ·1989-02-00 ·Pages 404-6

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

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.

MeSH Terms
Chromatography, High Pressure Liquid Drug Stability Epidermal Growth Factor/analysis Humans Recombinant Proteins/analysis Solutions
Chemicals
Recombinant Proteins Solutions Epidermal Growth Factor
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Araki F
Nakamura H
Nojima N
Tsukumo K
Sakamoto S
Article Info
Journal
Chemical & pharmaceutical bulletin
Abbr.
Chem Pharm Bull (Tokyo)
ISSN
0009-2363
Published
1989-02-00
Pages
404-6
Language
English
Region
Japan
NLM ID
0377775
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com