Summary
Free radicals species can modify proteins as well as lipids. In vitro study of protein oxidation involves the evaluation of amino acid degradation, bityrosine production as well as structural modifications of proteins. The protein electrophoresis is relevant to determine protein aggregation and/or protein fragmentation. The change of protein solubility is linked to the modifications of their secondary and tertiary structure. Direct evidence of protein conformational changes secondary to free radical attack can be obtained with X-ray diffraction studies.
However, few methods are available in clinical chemistry to evaluate in vivo protein free radical attack. The measurement of sulfhydryl and carbonyl are an interesting way to evaluate the free radical attack of plasma protein. These measurements involve a spectrophotometric method using respectively for thiol and carbonyl groups 5,5’-dithio-bis(2-nitrobenzoic acid) and 2,4-dinitrophenylhydrazine.
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© 1995 Birkhäuser Verlag Basel/Switzerland
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Faure, P., Lafond, JL. (1995). Measurement of plasma sulfhydryl and carbonyl groups as a possible indicator of protein oxidation. In: Favier, A.E., Cadet, J., Kalyanaraman, B., Fontecave, M., Pierre, JL. (eds) Analysis of Free Radicals in Biological Systems. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-9074-8_17
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