A three-step purification method of large quantities of human recombinant a endothelial cellular growth factor for clinical use
Sauter, Alexander, Lambert, Katherine L., Rupf, Ann-Katrin, Von Specht, Bernd-Ulrich, Hoermann, Karl and Naim, Ramin. (2007) A three-step purification method of large quantities of human recombinant a endothelial cellular growth factor for clinical use. International Journal of Molecular Medicine, Volume 19 (Number 1). pp. 97-103. ISSN 1107-3756Full text not available from this repository.
The endothelial cellular growth factor alpha-ECGF is a candidate drug for the induction of therapeutic neoangiogenesis. Its use in extensive experimental and clinical trials is hampered by the fact that currently published purification procedures allow only small yields, and the absence of pyrogenic impurities is not demonstrated. The rh alpha-ECGF was expressed in E. coli. Isolation of rh alpha-ECGF from E. coli lysates to apparent homogenicity was achieved by a three step purification procedure involving ionic exchange, heparin-sepharose and polymyxin B chromatography. By this method, 200 mg of rh alpha-ECGF was purified from 15 g wet weight E. coli bacteria. The isolated protein of 18 kDa appeared as a single band after SDS gel electrophoresis and subsequent silver-staining. The biological activity was expressed in the chorion-allantois-membrane assay and in the H-3-thymidine proliferation in baby hamster kidney cells. Drug trials with rabbits revealed no increase in body temperature after intravenous injections with 1 mg rh-ECGF.
|Item Type:||Journal Article|
|Journal or Publication Title:||International Journal of Molecular Medicine|
|Number of Pages:||7|
|Page Range:||pp. 97-103|
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