Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10801043 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2005 | 8 Pages |
Abstract
Fat-free bovine milk fermented by 12 kinds of lactic acid bacteria and yeast enhanced monoclonal antibody production of human hybridoma HB4C5 cells 2.8-fold in serum-free medium. Immunoglobulin production of human peripheral blood lymphocytes (PBL) was also stimulated in vitro. IgM and IgG production of human PBL was accelerated up to 2.8-fold and 5.4-fold, respectively. Interferon-γ production of human PBL was also accelerated 6.0-fold by 50 μg/ml of the fermented milk. However, interleukin-4 production of PBL was not affected, and tumor necrosis factor-α production was suppressed. The activity was enhanced 2.5-fold by the thermal treatment for 30 min at 65 °C and was completely lost by trypsin digestion. The findings suggested that the active substance in the fermented milk was heat stable protein. Gel-filtration and the SDS-PAGE analysis revealed that the molecular weight of the active substance was estimated as 19.0 kDa, which was not detected in fat-free bovine milk before fermentation. N-terminal amino acid sequence of the 19.0 kDa protein was highly homologous to proteose-peptone component 3 (PP3). Since molecular weight of PP3 is 28 kDa, it is suggested that the 19.0 kDa protein is derived from degradation of PP3 during fermentation of fat-free milk. Moreover, PP3 purified from fat-free milk also enhanced IgM production of HB4C5 cells.
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Authors
Takuya Sugahara, Hiroyuki Onda, Yusuke Shinohara, Mayumi Horii, Koichi Akiyama, Katsunori Nakamoto, Kazushi Hara,