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PubMed1983

Individual quantitation of vitamin D2, vitamin D3, 25-hydroxyvitamin D2, and 25-hydroxyvitamin D3 in human milk.

Extraction, lipid-reduction, and chromatographic methods suitable for the resolution and subsequent quantitation of vitamin D2, vitamin D3, 25-hydroxyvitamin D2, and 25-hydroxy-vitamin D3 from human milk are described. This procedure utilizes a methanol:methylene chloride extraction, precipitation of unwanted lipids with cold methanol and ether, backwash with alkaline buffer, silica Sep-Pak preparative chromatography, normal- and reverse-phase high-performance liquid chromatography with final quantitation of the antirachitic sterols by competitive protein binding assay. The described assay was used to determine these antirachitic sterols in milk from women receiving various supplements of vitamin D or undergoing ultraviolet phototherapy.

Cholecalciferol↗
PubMed1987

Use of Fourier transform 1H NMR in the identification of vitamin D2 metabolites.

The use of Fourier transform 1H NMR to characterize vitamin D2 metabolites is described. A 300-MHz spectrometer capable of generating a 6-microseconds pulse and a sweep width of 4000 Hz was used. High-resolution spectra were obtained on 5 micrograms of material using standard 5-mm NMR tubes fitted with glass inserts and isotopically enriched chloroform-d solvent. The data acquisition time under these conditions was 4 h. Application of this technique to a variety of both synthetic and naturally occurring vitamin D2 metabolites, in addition to synthetic delta 22-1,25-dihydroxyvitamin D3, resulted in the reassignment of the chemical shifts for the C-21 and C-28 methyl groups of vitamin D2. The C-21 methyl group resonance is now assigned to the doublet appearing at delta 1.01, whereas the C-28 signal corresponds to the doublet at delta 0.90. An examination of the spectrum of 24 (R),25-dihydroxyvitamin D2 also led to the reassignment of the side-chain methyl group resonances. This technique is an additional means of identifying microgram quantities of vitamin D metabolites.

Ergocalciferols↗
PubMed1987

Synthesis of 25-hydroxy-[26,27-3H]vitamin D2, 1,25-dihydroxy-[26,27-3H]vitamin D2 and their (24R)-epimers.

Synthesis of a C-24-epimeric mixture of 25-hydroxy-[26,27-3H]vitamin D2 and a C-24-epimeric mixture of 1,25-dihydroxy-[26,27-3H]vitamin D2 by the Grignard reaction of the corresponding 25-keto-27-nor-vitamin D2 and 1 alpha-acetoxy-25-keto-27-nor-vitamin D3 with tritiated methyl magnesium bromide is described. Separation of epimers by high-performance liquid chromatography afforded pure radiolabeled vitamins of high specific activity (80 Ci/mmol). The identities and radiochemical purities of 25-hydroxy-[26,27-3H[vitamin D2 and 1,25-dihydroxy-[26,27-3H]vitamin D2 D2 were established by cochromatography with synthetic 25-hydroxyvitamin D2 or 1,25-dihydroxyvitamin D2. Biological activity of 25-hydroxy-[26,27-3H]vitamin D2 was demonstrated by its binding to the rat plasma binding protein for vitamin D compounds, and by its in vitro conversion to 1,25-dihydroxy-[26,27-3H]vitamin D2 by kidney homogenate prepared from vitamin D-deficient chickens. The biological activity of 1,25-dihydroxy-[26,27-3H]vitamin D2 was demonstrated by its binding to the chick intestinal receptor for 1,25-dihydroxyvitamin D3.

25-Hydroxyvitamin D 2↗
PubMed1984

The isolation and identification of vitamin D2 and vitamin D3 from Medicago sativa (alfalfa plant).

Vitamin D2 and vitamin D3 were isolated from Medicago sativa (alfalfa) grown under field and laboratory conditions and then irradiated with ultraviolet light. The vitamins were identified by ultraviolet absorption, mass spectroscopy, and comparison with synthetic standards on several chromatographic systems. Sun-cured, field-grown alfalfa contained vitamin D2 at a concentration of 48 ng/g (1920 IU/kg) and vitamin D3 at 0.63 ng/g (25 IU/kg). Laboratory-grown alfalfa, artificially irradiated, contained vitamin D2 at a concentration of 80 ng/g and vitamin D3 at 1.0 ng/g. Therefore, the presence of vitamin D2, as well as vitamin D3, has unequivocally been demonstrated in alfalfa plant tissue.

Chemical Phenomena↗
PubMed1989

Comparison of receptor binding, biological activity, and in vivo tracer kinetics for 1,25-dihydroxyvitamin D3, 1,25-dihydroxyvitamin D2, and its 24 epimer.

Scatchard analyses of 1,25-dihydroxyvitamin D receptors (VDR) from chick and rat intestine, bovine thymus, pig kidney cells (LLC-PK1), and human breast cancer cells (T-47D) demonstrated that 1,25-dihydroxyvitamin D3 (1,25-D3) and 1,25-dihydroxyvitamin D2 (1,25-D2) had equal affinities for VDR. 24-Epi-1,25-dihydroxyvitamin D2 (24-epi-1,25-D2) exhibited affinities for VDR equal to that of 1,25-D2 and 1,25-D3 in most of these tissues. Scatchard analysis with 24-epi-[3H]1,25-D2 underestimated total VDR by 50-70% in rat intestine, LLC-PK1, and T-47D cells. The biological activity of 24-epi-1,25-D2 was found to be only 30-70% of 1,25-D3 and 1,25-D2 as determined by in vivo induction of intestinal calcium transport and bone calcium resorption in the rat and in vitro induction of 23- and 24-hydroxylase activities in T-47D cells. In vivo tracer kinetic studies demonstrated that in the rat 1,25-D3 and 1,25-D2 kinetics were similar, whereas 24-epi-1,25-D2 had a 25% shorter plasma half-life and was cleared from the body 2.8 times faster than the natural hormones. This more rapid clearance of 24-epi-1,25-D2 along with reduced VDR binding appears to explain the reduced biological activity of 24-epi-1,25-D2. Our data clearly demonstrate that although there are differences in side chain structure between 1,25-D2 and 1,25-D3, the VDR binding, biological activity, and whole body tracer kinetics of these two metabolites are virtually identical. However, movement of the 28 methyl of 1,25-D2 from its natural S configuration to the R configuration significantly alters the activity of this hormone.

Animals↗
PubMed1989

Metabolism of vitamin D2 in pig liver homogenates: evidence for a free radical reaction.

In vitro hydroxylation of vitamin D2 at carbon-24 (C-24) was demonstrated with pig liver homogenate. The putative 24-hydroxyvitamin D2 (24-OHD2) comigrated with standard 24-OHD2 on a Zorbax Sil column developed in hexane/isopropanol (98/2). Rechromatography in methylene chloride/methanol (99.8/0.2) resolved the putative 24-OHD2 into two components. The identity of these compounds was determined to be 24(R)-OHD2 and 24(S)-OHD2 (epimers) by low resolution mass spectroscopy and proton NMR spectroscopy. The fact that epimers of 24-OHD2 were produced from vitamin D2 in the absence of pig liver homogenate in vitro was strong evidence for the participation of free radicals in the reaction. Further support for free radical involvement was provided by the following observations: (a) hydroxyl free radical scavengers such as alpha-tocopherol, catalase, and ethanol reduced the amount of 24-OHD2 produced by 18-64%; (b) use of autoclaved homogenate in the incubation mixture had little or no effect on the amount of 24-OHD2 produced; and (c) the failure of the enzyme-substrate saturation curve to level off as expected with high levels of vitamin D2 (100-2000 micrograms = 50-1009 microM). Maximum production of 24-OHD2 was obtained at pH 4.75 and represented a sevenfold increase relative to the amount produced at pH 7.4. The omission of citrate or the addition of electron transport inhibitors, cyanide or antimycin, had little or no effect on the reaction. These data suggested that C-24 hydroxylation of vitamin D2 in vitro was a free radical-mediated process not involving the electron transport system. In vitro hydroxylation at C-24 appeared to be driven by free radicals, and the dominance of this reaction made it difficult to determine whether there was an enzyme involved in the reaction.

Animals↗