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Human serum albumin was subjected to oxidative stress under metal-catalyzed oxidation (MCO) conditions or by treatment with hypochlorous acid (HOCl), and the locations of the resulting protein carbonyls were determined using mass spectrometry. Under MCO conditions, only two of the 59 lysine residues appeared to be modified (97Lys and 186Lys). With HOCl, five different lysine modification sites were identified (130Lys, 257Lys, 438Lys, 499Lys, and 598Lys) [ Temple, A., Yen, . & Gronert, S. (2006) Identification of sites of carbonylation. Amer. Soc. Mass Spect. 17, 1172-1180]. Low concentrations of chloramine-T oxidize 34Cys and methionine residues; at higher concentrations the tryptophan residue also appears to be oxidized [ Anraku, M., Kragh-Hansen, U., Kawai, K., Maruyama, T., Yamasaki, Y., Takakura, Y. & Otagiri, M. (2003) Validation of the chloramine-T induced oxidation of human serum albumin as a model for oxidative damage in vivo. Pharm. Res. 20, 684-692]. A study with recombinant albumins and a series of oxidizing agents showed in a direct way that 34Cys plays a more important role than the methionine residues in the antioxidant activity of albumin [ Iwao, Y., Ishima, Y., Yamada, J., Noguchi, T., Kragh-Hansen, U., Mera, K., Honda, D., Suenaga, A., Maruyama, T. & Otagiri, M. (2012) Quantitative evaluation of the role of cysteine and methionine residues in the antioxidant activity of human serum albumin using recombinant mutants. IUBMB Life 64, 450-454]. Diabetes mellitus, liver diseases and nephropathy are just a few examples of disorders in which oxidative stress is involved, and altered albumin functions have been described. See the reviews: (1) Oettl, K. & Stauber, . (2007) Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties. Brit. J. Pharmacol. 151, 580-590; (2) Anraku, M., Chuang, ., Maruyama, T. & Otagiri, M. (2013) Redox properties of serum albumin. Biochim. Biophys. Acta 1830, 5465-5472; (3) Bruschi, M., Candiano, G., Santucci, L. & Ghiggeri, . (2013) Oxidized albumin. The long way of a protein of uncertain function. Biochim. Biophys. Acta 1830, 5473-5479.

Debolt properties

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