Demott B J, Dincer B
J Dairy Sci. 1976 Sep;59(9):1557-9. doi: 10.3168/jds.S0022-0302(76)84404-9.
Binding of an added radionuclide to milk protein and casein components of cow's milk fractionated by the combination of Sephadex G-150 gel filtration and diethylaminoethyl-cellulose chromatography was determined. Iron-59 labeled ferric chloride was added directly to raw whole milk at a concentration of .02 and 10 ppm isotope and carrier, respectively, and held overnight at 4 C. Five milliliters of the skin milk were chromatographed on a Sephadex G-150 column and fractionated into casein, whey protein, and nonprotein materials. The casein fraction was chromatographed on a diethylaminoethyl-cellulose column and separated into its components, alphas-, beta-, and kappa-caseins. Casein bound about 85% of the added iron in skim milk; of this amount, 72, 21, and 4% were associated with the alphas-, beta, and kappa-caseins.
通过葡聚糖凝胶G - 150凝胶过滤和二乙氨基乙基纤维素色谱法相结合对牛奶进行分级分离，测定了添加的放射性核素与牛奶中乳蛋白和酪蛋白成分的结合情况。分别以0.02 ppm和10 ppm的同位素及载体浓度，将铁 - 59标记的氯化铁直接添加到生鲜全脂牛奶中，并在4℃下保存过夜。取5毫升脱脂牛奶在葡聚糖凝胶G - 150柱上进行色谱分析，分离成酪蛋白、乳清蛋白和非蛋白物质。酪蛋白部分在二乙氨基乙基纤维素柱上进行色谱分析，并分离成其组分，即α -、β - 和κ - 酪蛋白。酪蛋白结合了脱脂牛奶中约85%添加的铁；其中，72%、21%和4%分别与α -、β - 和κ - 酪蛋白相关。
