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...

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Bibliographic Details
Published inRussian journal of bioorganic chemistry Vol. 26; no. 6; pp. 375 - 380
Main Authors Trubetskaya, O. E., Reznikova, O. I., Afanas’eva, G. V., Reznikov, K. Yu, Serebryakova, M. V.
Format Journal Article
LanguageEnglish
Published New York Springer Nature B.V 2000
Subjects
Bonding
Fluorescent dyes
Glycoproteins
Proteins
Residues
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Summary: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.
ISSN:1068-1620
1573-9163
1608-330X
DOI:10.1007/BF02758664