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Journal of Clinical Endocrinology & Metabolism, Vol 50, 773-775, Copyright © 1980 by Endocrine Society

ARTICLES

Displacement potency of vitamin D2 analogs in competitive protein- binding assays for 25-hydroxyvitamin D3, 24,25-dihydroxyvitamin D3, and 1,25-dihydroxyvitamin D3

G Jones, B Byrnes, F Palma, D Segev and Y Mazur

24(R),25-Dihydroxyergocalciferol [24,25-(OH)2-D2] is 1.7 times less potent than 24 (R), 25-(OH)2D3, 25-Hydroxyvitamin D2 (25OHD2), or 25OHD3 in the displacement of (3H)25OHD3 from rat serum binding proteins. 1,25-(OH)2D2 is 1.3 times less potent than 1,25-(OH)2D3 in the displacement of (3H)1,25-(OH)2D3 from a chick intestinal binding receptor. In light of binding affinity and chromatographic differences between vitamin D3 and its D2 analogs, it is our view that methods which purport to measure 1,25-(OH)2D and 24,25-(OH)2D probably understimate the contributions of D2 metabolites. This is particularly important in the case of plasma extracts from patients given large doses of vitamin D2.


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