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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

Russian Journal of Bioorganic Chemistry volume 26, pages 375–380 (2000)Cite this article

Abstract

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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Abbreviations

AGP:

al-acid glycoprotein

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Authors and Affiliations

  1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry (Pushchino Branch), Russian Academy of Sciences, 142292, Pushchino, Moscow oblast, Russia

    O. E. Trubetskaya, O. I. Reznikova, G. V. Afanas’eva & K. Yu. Reznikov

  2. Research Center of Mental Health, Russian Academy of Medical Sciences, Moscow

    M. V. Serebryakova

Authors
  1. O. E. Trubetskaya
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  2. O. I. Reznikova
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  3. G. V. Afanas’eva
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  4. K. Yu. Reznikov
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  5. M. V. Serebryakova
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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). https://doi.org/10.1007/BF02758664

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  • DOI: https://doi.org/10.1007/BF02758664

Key words

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