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Enhancing effect of malondialdehyde modification on the mouse IgE response to protein antigens
H Tani1, T Matsuda, R Nakamura
1Department of Food Science and Technology, School of Agriculture, Nagoya University, Japan.
To investigate the immunochemical properties of proteins reacted with malondialdehyde (MDA), which is a major degradation product of lipid oxidation, the antibody responses of mice immunized with MDA-modified bovine serum albumin (BSA) were examined. The specific IgE response to MDA-BSA was 4 to 8 times higher than that to native BSA, suggesting that the specific IgE antibody response to MDA-modified protein was enhanced by MDA bound to the surface of the protein. The antibodies to MDA-BSA did not distinguish the modified protein from the native one, and the antibodies raised against the modified proteins were not specific for the MDA portion but were for the carrier proteins.
To investigate the immunochemical properties of proteins reacted with malondialdehyde (MDA), which is a major degradation product of lipid oxidation, the antibody responses of mice immunized with MDA-modified bovine serum albumin (BSA) were examined. The specific IgE response to MDA-BSA was 4 to 8 times higher than that to native BSA, suggesting that the specific IgE antibody response to MDA-modified protein was enhanced by MDA bound to the surface of the protein. The antibodies to MDA-BSA did not distinguish the modified protein from the native one, and the antibodies raised against the modified proteins were not specific for the MDA portion but were for the carrier proteins.