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Anticancer activity of hydrophobic peptides from soy proteins
Author(s) -
Kim Song E,
Kim Hyuck Hwa,
Kim Ji Yeon,
Kang Young Im,
Woo Hee Jong,
Lee Hyong Joo
Publication year - 2000
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.5520120124
Subject(s) - sephadex , peptide , chemistry , size exclusion chromatography , chromatography , in vitro , hydrolysis , soy protein , cytotoxicity , biochemistry , high performance liquid chromatography , ic50 , ethanol , cell culture , enzyme , biology , genetics
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. IC 50 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.