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Journal of Clinical Endocrinology & Metabolism Vol. 43, No. 1 86-91
doi:10.1210/jcem-43-1-86
Copyright © 1976 by the Endocrine Society.
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Human Serum Binding Capacity and Affinity for 25-Hydroxyergocalciferol and 25-Hydroxycholecalciferol

JOHN G. HADDAD, LAURA HILLMAN and SOMKIETR ROJANASATHIT

The Department of Medicine and Pediatrics, Washington University School of Medicine St. Louis Children's Hospital of St. Louis, Mo. 63110

25-Hydroxyvitamin D-binding capacity and affinity were studied in human cord, adult, and maternal sera, and in sera from women receiving oral contraceptives, by in vitro saturation analyses employing dextran-coated charcoal to adsorb unbound sterol. 25-Hydroxyergocalciferol and 25-hydroxycholecalciferol were equipotent in their ability to displace 3H 25-hydroxycholecalciferol from human serum binding sites. At 0 C, the apparent dissociation constant for the serum binding of 25-hydroxycholecalciferol was low (Kd = 8 x 10–10M). Cord and adult sera had a similar 25-hydroxycholecalciferol binding capacity (1.8 x 10–6), but the binding capacity of maternal sera and the sera from women receiving oral contraceptives was significantly higher. At physiological serum concentrations of 25-hydroxyvitamin D (5 x 10–8), only 2–3% of human serum 25-hydroxyvitamin D-binding sites are occupied.

Received December 29, 1975.







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Copyright © 1976 by The Endocrine Society