Abstract
This study investigated the stability of myoglobin under different temperatures and sodium dodecyl sulfate (SDS) concentrations. The conformational changes of the protein embedded in SDS with different pH (2, 4.5, and 7.4) and temperature (from 30°C to 100°C) were evaluated using absorption and fluorescence spectroscopy methods. Results indicated that increasing the SDS concentration increased the stability of myoglobin at pH 2 and 4.5, while pH 7.4 had a negative influence on the stability of myoglobin processes. Fluorescence intensities decreased at 50°C and 60°C in pH 2, while they increased at 30°C, 40°C, and 50°C in pH 7.4. The intensity of fluorescence at pH 4.5 remained constant without detectable changes throughout the experiment. In conclusion, increasing pH increased T m occurred, and therefore, the stability of native myoglobin also increased. Myoglobin denaturation with SDS led to an increase in the myoglobin stability at pH 2 and 4.5 and a decrease of the myoglobin stability at pH 7.4.
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Acknowledgment
The authors greatly appreciate the support of this research by the Payamnoor University of Tehran, Iran. The authors thank Zahra Hashemi and Azardokht Reeisi for their help in the biochemistry laboratory.
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Shareghi, B., Nazem, H., dehkordi, Z.K. et al. Studies on the stability of myoglobin in the presences of sodium dodecyl sulfate (SDS) and temperature. Comp Clin Pathol 19, 141–145 (2010). https://doi.org/10.1007/s00580-009-0840-9
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DOI: https://doi.org/10.1007/s00580-009-0840-9