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Localization of disulfide bonds in α1-acid glycoprotein and their effect on the ability of the protein to interact with ethidium bromide


α1-Acid glycoprotein (orosomucoid) was purified from the human and murine blood sera using phenol deproteinization. As opposed to the murine protein, the human orosomucoid bound the fluorescent dye ethidium bromide but lost this ability after treatment with β-mercaptoethanol, which breaks disulfide bonds. Disulfide bonds between the Cys23 and Cys165 residues of the human orosomucoid and between the Cys91 and Cys184 residues of the murine orosomucoid were identified.

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al-acid glycoprotein


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Correspondence to O. E. Trubetskaya.

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Trubetskaya, O.E., Reznikova, O.I., Afanas’eva, G.V. et al. Localization of disulfide bonds in α1-acid glycoprotein and their effect on the ability of the protein to interact with ethidium bromide. Russ J Bioorg Chem 26, 375–380 (2000).

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Key words

  • α1-acid glycoprotein
  • orosomucoid
  • acute-phase blood serum proteins