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- W1966656321 abstract "1. Following in vivo administration to human subjects, 25-[3H]hydroxycholecalciferol in their plasma was found to be eluted from DEAE-cellulose columns with 0.1 M sodium phosphate (pH 5.8). Similar fractions from in vitro labelled plasma were filtered on Sephadex G-100, and polyacrylamide disc gel electrophoresis showed a heterogeneous preparation in which 85% of the 25-[3H]hydroxycholecalciferol was bound to an inter-α globulin, and < 10% associated with the major protein constituent, albumin. 2. The molecular weight of the binding protein was 40000–45000, as estimated by its elution from Sephadex G-100 columns. Sucrose density ultracentrifugation revealed the [3H]sterol-protein complex to have a sedimentation coefficient of 3.1 S. 3. Competitive displacement of 25-[3H]hydroxycholecalciferol by various sterols revealed the following order of decreasing potency: 25-hydroxycholecalciferol >cholecalciferol >ergocalciferol. 7-Dehydrocholesterol, cortisol and cholesterol were not found to be competitive. 4. The protein-sterol complex was reversibly dissociated by increased temperature. Specific binding ability was irreversibly lost following exposure to 65°, pH 3.0 solutions, trypsin and neuraminidase." @default.
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- W1966656321 date "1971-12-01" @default.
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- W1966656321 title "25-Hydroxycholecalciferol-binding globulin in human plasma" @default.
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- W1966656321 doi "https://doi.org/10.1016/0005-2760(71)90237-2" @default.
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