An electrophoretic method is described for estimating the saturation of serum transferrin. After first precipitating most of the other proteins with Rivanol, the apo-, mono-, and di-ferric transferrins are separated by electrophoresis in urea-polyacrylamide gel. Densitometric scanning enables the percentage saturation to be calculated.
References
1.
HuismanW. Interference of Imferon in colorimetric assays for iron. Clin Chem1980; 26: 635–7.
2.
EvansRWWilliamsJ. Studies of the binding of different iron donors to human serum transferrin and isolation of iron binding fragments from the N- and C-terminal regions of the protein. Biochem J1978; 173: 543–52.
3.
MakeyDGDealUD. The detection of four molecular forms of human transferrin during the iron binding process. Biochim Biophys Acta1976; 453: 250–6.
4.
LeibmanAAisenP. Distribution of iron between the binding sites of transferrin in serum. Methods and results in normal human studies. Blood1979; 53: 1058–65.
5.
SaganZ. The application of Rivanol for serum transferrin and immunoglobulin G determination. Clin Chim Acta1968; 21: 225–30.
6.
StoakeyLL. Ferrozine—a new spectrophotometric reagent for iron. Anal Chem1970; 42: 779.
7.
ZakBEpsteinE. Automated determination of serum iron. Clin Chem1965; 11: 641–4.
8.
HorejsiJSmetanaR. Isolation of gamma globulin from blood serum by Rivanol. Acta Med Scand1956; 155: 65–70.
9.
WilliamsJMarstonK. The distribution of iron between the metal binding sites of transferrin in human serum. Biochem J1980; 185: 483–8.
10.
Van der HeulCVan EijkHGWillinkWFLeijnaeB. The binding of iron to transferrin and to other serum components at differing degrees of saturation with iron. Clin Chim Acta1972; 38: 347–53.
