Effect of gamma-irradiation on the molecular properties of myoglobin.
To elucidate the effect of gamma-irradiation on the molecular properties of myoglobin, the secondary and tertiary structures, as well as the molecular weight size of the protein, were examined after irradiation at various irradiation doses. Gamma-irradiation of myoglobin solutions caused the disruption of the ordered structure of the protein molecules, as well as degradation, crosslinking, and aggregation of the polypeptide chains. A SDSPAGE 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 protected against the degradation and aggregation of proteins by scavenging oxygen radicals that are produced by irradiation. A circular dichroism study showed that an increase of the irradiation decreased the alpha-helical content of myoglobin with a concurrent increase of the aperiodic structure content. Fluorescence spectroscopy indicated that irradiation increased the emission intensity that was excited at 280 nm.
Lee
Yongwoo
Y
Department of Food Science and Technology, College of Agriculture and Life Sciences, Chungnam National University, Taejon 305-764, Korea.
Song
Kyung Bin
KB
D000818:Animals; D001205:Ascorbic Acid / Q000378:metabolism / Q000494:pharmacology; D002942:Circular Dichroism; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D005720:Gamma Rays; D006736:Horses; D009211:Myoglobin / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D014466:Ultraviolet Rays
D003432:Cross-Linking Reagents; D009211:Myoglobin; D001205:Ascorbic Acid