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Expression of recombinant epidermal growth factor inE. coli

โœ Scribed by Chang Shin Yoon; Eun Gyu Lee; Young Seek Lee; Il Yup Chung

Publisher
The Korean Society for Biotechnology and Bioengineering
Year
1997
Tongue
English
Weight
535 KB
Volume
2
Category
Article
ISSN
1226-8372

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Rapid purification and partial character
Rapid purification and partial characterization of recombinant human epidermal growth factor produced byEscherichia coli
โœ V. B. Yadwad; K. Meghji; O. P. Ward ๐Ÿ“‚ Article ๐Ÿ“… 1993 ๐Ÿ› Springer-Verlag ๐ŸŒ English โš– 542 KB

Human recombinant EGF, secreted into the extracellular medium by E. c&i cells, was purified by a combination of solid phase extraction and HPLC. Using these techniques, the peptide was purified 122-fold, with a recovery of greater than 75%. The purified hEGF manifested no contaminating protein bands