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• W1576451296 abstract "Abstract Testosterone-estradiol-binding globulin in human plasma was characterized and quantified by polyacrylamide gel electrophoresis. Testosterone and estradiol were shown to bind to a single homogeneous protein over a wide range of experimental conditions. Testosterone binding to cortisol-binding globulin (transcortin) and estradiol binding to albumin were clearly demonstrated; both transcortin and albumin were separated from testosterone-estradiol-binding globulin by polyacrylamide gel electrophoresis, as was transferrin, a serum protein similar to testosterone-estradiol-binding globulin with respect to size and charge. The molecular, radius, apparent molecular weight, and net charge of testosterone-estradiol-binding globulin were obtained at three different pH values at 0°. A molecular radius of 2.95 nm was estimated and a molecular weight of 98,000 was computed with the use of a partial specific volume of 0.66. These values were independent of the presence or absence of ligand and were also obtained in urea concentrations up to 4 m. Testosterone-estradiol-binding globulin capacity was routinely determined with 5α-dihydrotestosterone-5H as a ligand because of its high affinity for the protein. Binding capacities in plasma expressed as micrograms of steroid bound per 100 ml were men, 0.49 ± 0.04 (S.E.); women, 1.42 ± 0.22; pregnancy, 10.91 ± 0.74; estrogen-treated women, 10.70 ± 1.04. The usefulness of polyacrylamide gel electrophoresis for the study of steroid-binding and other binding proteins in biological fluids or tissues is discussed." @default.
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• W1576451296 date "1971-06-01" @default.
• W1576451296 modified "2023-10-03" @default.
• W1576451296 title "Physical Properties and Binding Capacity of Testosterone-Estradiol-binding Globulin in Human Plasma, Determined by Polyacrylamide Gel Electrophoresis" @default.
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• W1576451296 doi "https://doi.org/10.1016/s0021-9258(18)62149-0" @default.
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