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Optimization of the solubilization and renaturation of fish growth hormone produced byEscherichia coli

โœ Scribed by M.-H. Hsih; J.-C. Kuo; H.-J. Tsai


Book ID
105954166
Publisher
Springer
Year
1997
Tongue
English
Weight
795 KB
Volume
48
Category
Article
ISSN
1432-0614

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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