KMID : 1007520030120040425
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Food Science and Biotechnology 2003 Volume.12 No. 4 p.425 ~ p.429
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Effect of ¥ã-Irradiation on the Molecular Properties of Hemoglobin
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Lee Seunghwan
Song Kyung-Bin
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Abstract
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To elucidate the effect of gamma-irradiation on the molecular properties of hemoglobin, the secondary, and tertiary structures of the protein, and its molecular weight were examined after irradiation at 0.5, 1, 5, and 10k§í. Gamma-irradiation of hemoglobin solutions caused the disruption of the ordered structure of the protein molecules, as well as degradation, cross-linking and aggregation of the polypeptide chains. A SDS-PAGE study indicated that irradiation caused initial fragmentation of the proteins and subsequent aggregation due to cross-linking of the protein molecules. The effect of irradiation on the protein was more significant at lower protein concentrations. Ascorbic acid decreased the degradation and aggregation of proteins by scavenging oxygen radicals that were produced by irradiation. A circular dichroism study showed that irradiation decreased the ¥á-helical content of hemoglobin with a concurrent increase of the aperiodic structure content. Fluorescence spectroscopy indicated that irradiation decreased the emission intensity that was excited at 280§¬.
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