Effect of γ-irradiation on the molecular properties of myoglobin

86Citations
Citations of this article
39Readers
Mendeley users who have this article in their library.

Abstract

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, 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 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 α-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. © BSRK & Springer-Verlag 2002.

Cite

CITATION STYLE

APA

Lee, Y., & Kyung, B. S. (2002). Effect of γ-irradiation on the molecular properties of myoglobin. Journal of Biochemistry and Molecular Biology, 35(6), 590–594. https://doi.org/10.5483/bmbrep.2002.35.6.590

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free