[Localization of disulfide bonds in the alpha 1 acidic glycoprotein molecule and study of their effect on ability of the protein to interact with ethidium bromide].
alpha 1-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 beta-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.
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Pushchino Branch, Russian Academy of Sciences, Moscow oblast, Russia. trub@fibkh.serpukhov.su
O E
OE
Trubetskaia
O I
OI
Rezinkova
G V
GV
Afanas'eva
K Iu
KIu
Reznikov
M V
MV
Serebriakova
D000595:Amino Acid Sequence; D000818:Animals; D004220:Disulfides / Q000737:chemistry*; D004996:Ethidium / Q000737:chemistry*; D006801:Humans; D008623:Mercaptoethanol / Q000737:chemistry; D051379:Mice; D008969:Molecular Sequence Data; D009961:Orosomucoid / Q000737:chemistry*
D004220:Disulfides; D009961:Orosomucoid; D008623:Mercaptoethanol; D004996:Ethidium