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자외선 조사가 Ovalbumin의 분자적 성질에 미치는 영향
조용식,송경빈,山田經路,한귀정 한국응용생명화학회 2008 Journal of Applied Biological Chemistry (J. Appl. Vol.51 No.4
To elucidate the effects of ultraviolet (UV) irradiation on molecular properties of ovalbumin, the molecular weight profile, secondary structure and tertiary structure of proteins were examined after irradiation by UV with 254 nm wavelength for 4, 8, 16 and 32 hrs, respectively. UV irradiation of protein solution caused the disruption on the native state of protein molecules. SDS-PAGE and gel permeation chromatography indicated that radiation caused initial fragmentation of polypeptide chains and as a result subsequent aggregation due to cross-linking of protein molecules. Circular dichroism (CD) study showed that UV irradiation caused the change on the secondary structure resulting in decrease of helical structure or compact denature on structure of protein depending on irradiation period. Fluorescence spectroscopy indicated that irradiation quenched the emission intensity excited at 280 nm. These results suggest that UV irradiation affect the molecular properties of ovalbumin and may have potential as a means to change the antigenicity of protein allergen. To elucidate the effects of ultraviolet (UV) irradiation on molecular properties of ovalbumin, the molecular weight profile, secondary structure and tertiary structure of proteins were examined after irradiation by UV with 254 nm wavelength for 4, 8, 16 and 32 hrs, respectively. UV irradiation of protein solution caused the disruption on the native state of protein molecules. SDS-PAGE and gel permeation chromatography indicated that radiation caused initial fragmentation of polypeptide chains and as a result subsequent aggregation due to cross-linking of protein molecules. Circular dichroism (CD) study showed that UV irradiation caused the change on the secondary structure resulting in decrease of helical structure or compact denature on structure of protein depending on irradiation period. Fluorescence spectroscopy indicated that irradiation quenched the emission intensity excited at 280 nm. These results suggest that UV irradiation affect the molecular properties of ovalbumin and may have potential as a means to change the antigenicity of protein allergen.
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