Anticancer activity of hydrophobic peptides from soy proteins
Article first published online: 16 DEC 2008
Copyright © 2000 International Union of Biochemistry and Molecular Biology, Inc.
Volume 12, Issue 1-4, pages 151–155, 2000
How to Cite
Kim, S. E., Kim, H. H., Kim, J. Y., Kang, Y. I., Woo, H. J. and Lee, H. J. (2000), Anticancer activity of hydrophobic peptides from soy proteins. BioFactors, 12: 151–155. doi: 10.1002/biof.5520120124
- Issue published online: 16 DEC 2008
- Article first published online: 16 DEC 2008
- thermoase hydrolyzates;
- soy protein
An anticancer peptide from soy protein was purified and isolated. Defatted soy protein was hydrolyzed with thermoase and hydrophobic peptides were extracted with ethanol. The peptide extract was fractionated by XAD-2 hydrophobic, gel filtration chromatography, and different C18 HPLCs. Anticancer activity of each fraction was assayed by measuring in vitro cytotoxicity on P388D1, a mouse monocyte macrophage cell line. IC50 value of a peptide fraction from Sephadex G-25 chromatography was 0.16 mg/ml. This peptide fraction at 1 mg/ml significantly affected cell cycle progression by arresting P388D1 at G2/M phases. Finally purified peptide from analytical C18 HPLC was nonapeptide of which molecular weight was 1157 Da and the sequence was X-Met-Leu-Pro-Ser-Tye-Ser-Pro-Tyr.