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At least 19 recordsLinked to original sources
PubMed1993

Effect of dietary contents of cholecalciferol, 1 alpha,25-dihydroxycholecalciferol and 24,25-dihydroxycholecalciferol on blood concentrations of 25-hydroxycholecalciferol, 1 alpha,25-dihydroxycholecalciferol, total calcium and eggshell quality.

1. Withdrawal of cholecalciferol (D3) supplement from a layers diet drastically reduced blood 25-hydroxycholecalciferol (25-OH-D3), 1 alpha,25-dihydroxycholecalciferol (calcitriol) and egg specific gravity (SG) within two weeks, followed by a decrease in blood total calcium (Ca). 2. Doubling the D3 supplement in the control diet (27.5 micrograms or 1100 IU/kg) almost linearly increased the circulating concentration of 25-OH-D3 without raising the concentration of calcitriol, Ca, or egg SG. 3. Replacing D3 by the optimal concentration of calcitriol (5 micrograms/kg diet) improved egg SG after 21 weeks of treatment without increasing blood calcitriol or total Ca. 4. By itself, 24,25-dihydroxycholecalciferol [24,25-(OH)2D3] was unable to maintain normal blood levels of calcitriol, Ca or egg SG and, when added together with calcitriol in the diet, tended to elevate blood Ca but suppress the beneficial effect of calcitriol on shell quality, with little or no effect on blood calcitriol.

24,25-Dihydroxyvitamin D 3↗
PubMed1983

The effects of 24R,25-dihydroxycholecalciferol and of 1 alpha,25-dihydroxycholecalciferol on ornithine decarboxylase activity and on DNA synthesis in the epiphysis and diaphysis of rat bone and in the duodenum.

The effect of cholecalciferol metabolites on ornithine decarboxylase activity and on DNA synthesis in developing long bones was investigated in vitamin D-depleted rats. In the epiphysis there was a 6.4-fold increase in ornithine decarboxylase activity 5 h after a single injection of 24R,25-dihydroxycholecalciferol but not of 24S,25-dihydroxycholecalciferol or other vitamin D metabolites. In comparison, in the diaphysis and duodenum, 1 alpha,25-dihydroxycholecalciferol, but not other vitamin D metabolites, caused a 3-3.5-fold increase in the enzyme activity. The enzyme activity in the tissues examined attained a maximal value at 5 h after the injection of the metabolites. The activity of ornithine decarboxylase in the epiphysial region increased dose-dependently as the result of a single injection of 24R,25-dihydroxycholecalciferol and attained a maximal value at a dose between 30 and 3000 ng. In addition, administration of 24R,25-dihydroxycholecalciferol, but not 24S,25-dihydroxycholecalciferol or other metabolites, caused within 24 h a 1.7-2.0-fold increase in [3H]thymidine incorporation into DNA of the epiphyses of tibial bones. In comparison, 1 alpha,25-dihydroxycholecalciferol caused a 1.5-fold increase in [3H]thymidine incorporation into DNA of the diaphyses and of the duodenum. The present data indicate that 24R,25-dihydroxycholecalciferol is involved in the regulation of epiphyseal growth, whereas 1 alpha,25,dihydroxycholecalciferol stimulates the proliferation of cells in the diaphysis of long bones and in the intestinal mucosa.

24,25-Dihydroxyvitamin D 3↗
PubMed1977

Binding properties of serum vitamin D transport proteins in vertebrates for 24R, 25-dihydroxycholecalciferol and 24S, 25-dihydroxycholecalciferol in vitro.

1. The affinities of the specific vitamin D plasma transport proteins for 25-hydroxycholecalciferol, 24R, 25-dihydroxycholecalciferol and 24S, 25-dihydroxycholecalciferol were studied in 34 vertebrate species. 2. Fish plasma proteins bound 25-hydroxycholecalciferol, 24R, 25-dihydroxycholecalciferol and 24S, 25-dihydroxycholecalciferol with equal efficiency. 3. Vitamin D transport proteins in birds and a monotreme bound 25-hydroxycholecalciferol more efficiently than 24R, 25-dihydroxycholecalciferol; in one bird the two seco-steroids were bound with equal efficiency. 4. Transport proteins from marsupial and placental mammals bound 24R, 25-dihydroxycholecalciferol more efficiently than 24S, 25-dihydroxycholecalciferol. 5. Twelve mammal transport proteins bound 25-hydroxycholecalciferol and 24R, 25-dihydroxycholecalciferol with equal efficiency, however, in six mammals 25-hydroxycholecalciferol was more efficiently bound.

24,25-Dihydroxyvitamin D 3↗
PubMed1971

Regulation by calcium of in vivo synthesis of 1,25-dihydroxycholecalciferol and 21,25-dihydroxycholecalciferol.

Tritiated 1,25-dihydroxycholecalciferol accumulates in several tissues, to an extent that varies with dietary calcium content, 12 hr after the administration of 325 pmoles of tritiated 25-hydroxycholecalciferol to rats. As the dietary and serum calcium concentrations increase, the amount of 1,25-dihydroxycholecalciferol is diminished and the concentration of 21,25-dihydroxycholecalciferol increases. This correlation is especially evident in rats given vitamin D(3). In vitamin D-deficient rats, the repression of 1,25-dihydroxycholecalciferol formation occurs with a diet containing 3% calcium and 20% lactose. The results suggest that the production of 1,25-dihydroxycholecalciferol, believed to be the metabolically active form of vitamin D in the intestine, is responsible for the adaptation of calcium absorption to low dietary concentrations of calcium.

Animals↗
PubMed1973

The stimulation of 1,25-dihydroxycholecalciferol metabolism in vitamin D-deficient rats by 1,25-dihydroxycholecalciferol treatment.

Daily oral administration of 1,25-dihydroxycholecalciferol to vitamin D-deficient rats increases the rate of disappearance of [(3)H]1,25-dihydroxycholecalciferol and increases the rate of appearance of metabolites both less polar and more polar than 1,25-dihydroxycholecalciferol in the intestine, bone, liver, kidney, plasma, and muscle. Since 1,25-dihydroxycholecalciferol is believed to be the metabolically active form of vitamin D in the stimulation of intestinal calcium transport and bone calcium mobilization, these results provide an explanation for the fact that daily oral administration of 1,25-dihydroxycholecalciferol is relatively ineffective in the maintenance of serum calcium and in the calcification of bone in rats.

Administration, Oral↗
PubMed1984

Stimulation of creatine kinase BB activity by 1 alpha,25-dihydroxycholecalciferol and 24R,25-dihydroxycholecalciferol in rat tissues.

Vitamin D metabolites stimulate creatine kinase BB activity in organs of vitamin D-deficient rats. In epiphyses of long bones, creatine kinase BB activity increases 2.6-fold 24 h after injection of 24R,25-dihydroxycholecalciferol but not of 1 alpha,25-dihydroxycholecalciferol. Contrariwise, 1 alpha,25-dihydroxycholecalciferol, but not 24R,25-dihydroxycholecalciferol, increases creatine kinase BB activity in diaphyses and in kidney. Neither metabolite affects creatine kinase activity in duodenal mucosa.

24,25-Dihydroxyvitamin D 3↗
PubMed1987

Synthesis of 1,25-dihydroxycholecalciferol and 24,25-dihydroxycholecalciferol by calvarial cells. Characterization of the enzyme systems.

The synthesis of 1,25-dihydroxycholecalciferol [1,25(OH)2D3] and 24,25-dihydroxycholecalciferol [24,25(OH)2D3] from 25-hydroxycholecalciferol [25(OH)D3] has previously been shown to occur in cells isolated from bone. The main findings of the present study are that the enzyme systems which catalyse these syntheses are: (1) active at 'in vitro' substrate concentrations over the range of 2-50 nM; (2) regulatable in a complex way by 1,25(OH)2D3, 24,25(OH)2D3, 25,26-dihydroxycholecalciferol and 25(OH)D3, but not by cholecalciferol ('vitamin D3'); and (3) have relatively short half-lives (approx. 5 h).

24,25-Dihydroxyvitamin D 3↗
PubMed1984

In vitro stimulation of articular chondrocyte differentiated function by 1,25-dihydroxycholecalciferol or 24R,25-dihydroxycholecalciferol.

The effects of 1,25-dihydroxycholecalciferol (1,25-(OH)2D3) (10(-13)M-10(-8) M) and 24R ,25-dihydroxycholecalciferol ( 24R ,25-(OH)2D3) (10(-12)M-10(-7) M) on cell proliferation and proteoglycan deposition were examined in our newly developed multilayer culture system for rabbit and human articular chondrocytes. The cells are embedded in an extracellular matrix similar to that seen in vivo and maintain their in vivo phenotype. We extracted and purified native proteoglycans and degraded material from three culture compartments: the medium, intercellular matrix, and cells. Proteoglycan synthesis and deposition were analyzed by measuring 35SO4 incorporation, hexuronic acid, and galactose contents. In both rabbit and human chondrocyte cultures, chronic 1,25-(OH)2D3 treatment inhibited chondrocyte proliferation and stimulated proteoglycan synthesis and accumulation in the three compartments at 10(-12)-10(-8) M; maximal effect was at 10(-10)M. Cell proliferation was reduced by 55% and the content of hexuronic acid (or galactose) was increased to about three times that of controls in all compartments. 1,25-(OH)2D3 did not alter the proteoglycan composition. Chronic 24R ,25-(OH)2D3 treatment induced comparable effects with a maximum at 10(-8)M. When human dermal fibroblasts were treated as above both vitamin D metabolites increase mitosis. 1,25-(OH)2D3 mainly reduced the pericellular deposition of proteoglycans, while 24R ,25-(OH)2D3 appeared to reduce their synthesis and deposition in both medium and pericellular compartments. These results suggest that both 1,25-(OH)2D3 and 24R ,25-(OH)2D3 act specifically on articular chondrocytes to promote phenotype expression.

Animals↗
PubMed1980

Effect of 1,25-dihydroxycholecalciferol and 1,25-dihydroxycholecalciferol glycoside on 2,3-diphosphoglycerate levels of the rat erythrocyte.

The erythrocytes of rats treated with 1, 25-dihydroxycholecalciferol or 1, 25-dihydroxycholecalciferol glycoside showed decreased levels of 2, 3-diphosphoglycerate. The same result has been obtained in vitro, indicating a direct effect of the sterol on the red cell. The glycoside is less active than the free sterol in vivo and more active in vitro. The decreased levels of diphosphoglycerate induced tissue hypoxia as shown by a higher plasma lactate/pyruvate ratio and a three fold increase in plasma erythropoietin concentration.

Animals↗
PubMed1981

Decreased 1,25-dihydroxycholecalciferol and increased 25-hydroxy- and 24,25-dihydroxycholecalciferol in tissues of rats treated with thyroxine.

The effect of thyroxine on the metabolism of vitamin D was investigated in rats. Vitamin D depleted rats were repleted by injections of radiolabelled cholecalciferol or 25-hydroxycholecalciferol (25OHD3). After 3 weeks, a state of hyperthyroidism was induced by daily injections of L-thyroxine for 21 days. The lipid extracts of the Plasma and tissues were analyzed by successive Sephadex LH-20 and high pressure liquid chromatography. The concentrations of 25OHD3 and of 24,25-dihydroxycholecalciferol (24,25 (OH)2D3) were significantly higher and those of cholecalciferol and of 1,25-dihydroxycholecalciferol (1,25(OH)2D3) were significantly lower in the plasma and tissues of animals treated with thyroxine than in controls. The present study suggests that alterations in the metabolism of vitamin D may be involved in the disturbances of calcium metabolism observed in hyperthyroidism.

24,25-Dihydroxyvitamin D 3↗
PubMed1982

In vitro action of 1,25-dihydroxycholecalciferol and 24,25-dihydroxycholecalciferol on matrix organization and mineral distribution in rabbit growth plate.

Growth plates of 18-day-old rabbits were incubated in a protein-free synthetic medium, either without any additive, with 1,25-dihydroxycholecalciferol [1,25-(OH)2D3] (10(-10) M), with 24,25-dihydroxycholecalciferol [24,25-(OH)2D3] (10(-10) M and 10(-9) M), with both metabolites, or with the ethanol solvent alone. Cartilages, before and after 5 days of incubation, were studied by light and electron microscopy. The intracellular calcium distribution was analyzed by the potassium pyroantimonate method, and the calcium content was verified by x-ray microprobe analysis. When compared to nonincubated samples the cartilages incubated for 5 days without any additive as well as the cartilages incubated with the solvent alone showed excessive hydratation and hypertrophy of the chondrocytes, which had lost their columnar arrangement. The matrix and the cells were devoid of mineral. The ultrastructure of the cells was well preserved. These changes were largely prevented by the presence of both vitamin D3 metabolites. With regard to calcium distribution, 1,25-(OH)2D3 maintained calcium in mitochondria and crystals in matrix vesicles, whereas 24,25-(OH)2D3 only partly maintained mitochondrial mineral. In the chondrocytes incubated with this latter metabolite, small calcium granules were seen in the cytoplasm; most vesicles were devoid of crystals, and amorphous precipitates were seen in the matrix. These data demonstrate the in vitro influence of vitamin D3 metabolites on the organization and mineralization of the cartilage matrix and on the distribution of intracellular calcium in chondrocytes. Furthermore, they support the hypothesis that the in vitro action of 1,25-(OH)2D3 is different from that of 24,25-(OH)2D3 in that 1,25-(OH)2D3 may influence calcium storage in mitochondria and matrix vesicles, whereas 24,25-(OH)2D3 is likely to be involved in calcium transport and release.

24,25-Dihydroxyvitamin D 3↗
PubMed1980

In vitro synthesis of 1 alpha,25-dihydroxycholecalciferol and 24,25-dihydroxycholecalciferol by isolated calvarial cells.

The question of whether the skeleton metabolizes 25-hydroxycholecalciferol [25(OH)D3] to more-polar products was studied. Calvarial cells were dispersed from 16-day old chicken embryos by using collagenase and then grown in culture in serum-free medium. Confluent cell cultures were incubated with 7 nM 25(OH)[3H]D3 for 2 hr, and the vitamin D metabolites were then extracted. At least four polar metabolites were produced. Based on separation by Sephadex LH-20 chromatography followed by high-pressure liquid chromatography, two of these metabolites were identified as 1,25-dihydroxycholecalciferol [1,25(OH)2D3] and 24,25-dihydroxycholecalciferol [24,25(OH)2D3]. These metabolites were also produced by cultured kidney cells but not by liver, heart muscle, or skin cells isolated from the same embryos. The specific activities of the calvarial 1- and 24-hydroxylases were similar in magnitude to those in isolated kidney cells. The specific activity of the calvarial 25(OH)D3:1-hydroxylase was inhibited by an 8-hr preincubation with 1,25(OH)2D3, whereas the 24-hydroxylase was enhanced. It is concluded that (i) vitamin D metabolism by isolated cells is organ-specific, (ii) calvarial cells produce active metabolites of vitamin D in significant amounts, (iii) vitamin D metabolism by calvarial cells is regulated by 1,25(OH)2D3, and (iv) locally produced, active metabolites could act locally, thereby adding a new dimension to the regulation of mineral metabolism by vitamin D metabolites.

25-Hydroxyvitamin D3 1-alpha-Hydroxylase↗
PubMed1983

Normal egg hatchability requires the simultaneous administration to the hen of 1 alpha,25-dihydroxycholecalciferol and 24R,25-dihydroxycholecalciferol.

A previous report [Science 201, 835-837 (1978)] presented evidence that the combined and simultaneous administration of the cholecalciferol (D3) metabolites 1 alpha,25-dihydroxycholecalciferol [1 alpha,25(OH)2D3] and 24R,25-dihydroxycholecalciferol [24R,25(OH)2D3] to White Leghorn hens was necessary for embryo development and normal egg hatchability; in the absence of 24R,25(OH)2D3 none of the fertile eggs hatched. The present study extends this fundamental observation to a second species, the Japanese quail, Coturnix coturnix japonica and compares the biological actions of the two stereoisomers of the 24,25(OH)2 metabolite, namely the naturally occurring 24R,25(OH)2D3 and its unnatural epimer 24S,25(OH)2D3. Groups of 12-14 vitamin D-depleted adult female Japanese quail were mated with normal male quail and eight consecutive batches of eggs (25-41 eggs from each group) were placed in an egg incubator, and egg hatchability for the fertile eggs monitored on days 21 and 22. The egg hatchability (in percent +/- SD) for each group was: D3 (56.5% +/- 12.8); 1 alpha,25(OH)2D3 (1.3% +/- 2.5); 24R,25(OH)2D3 (29.6% +/- 3.1); 24R25(OH)2D3 + 1 alpha,25-(OH)2D3 (32.8%); and 24S,25(OH)2D3 + 1 alpha,25(OH)2D3 (7.2%). Also for all treatment groups the blood level of the expected vitamin D metabolites were in the normal range, and there were no significant differences in the embryo weights and eggshell thickness (of both hatched and unhatched eggs). These results indicate that the Japanese quail have the inherent capability to discriminate between the stereoisomers of 24,25(OH)2D3 and therefore strongly support the concept that only the naturally occurring 24R,25(OH)2D3 has an identifiable, unique biological role which is different from that of 1 alpha,25(OH)2D3.

24,25-Dihydroxyvitamin D 3↗
PubMed1988

Differential effects of 1 alpha,25-dihydroxycholecalciferol and 24R,25-dihydroxycholecalciferol on the proliferation and the differentiated phenotype of rabbit costal chondrocytes in culture.

1 alpha,25-Dihydroxycholecalciferol [1,25-(OH)2D3] stimulated the proliferation and DNA synthesis of rabbit costal growth cartilage cells in the logarithmic growth phase in culture. The stimulatory effects of 1,25-(OH)2D3 were observable at a concentration of 10(-10) M and maximal at a concentration of 10(-8) M. On the other hand, 1,25-(OH)2D3 inhibited their expression of the cartilage phenotype, as judged morphologically, histochemically, and biochemically by a decrease in glycosaminoglycan (GAG) synthesis. The inhibition of GAG synthesis was also dose dependent and observable at a concentration of 10(-10) M. 1,25-(OH)2D3 also stimulated the proliferation of resting cartilage cells and inhibited their GAG synthesis, but its effects on these cells were less than those on growth cartilage cells, suggesting that 1,25-(OH)2D3 acts more specifically on growth cartilage cells than on resting cartilage cells. 1,25-(OH)2D3 had no effect on either DNA synthesis or GAG synthesis of growth cartilage cells in confluent cultures. 24R,25-Dihydroxycholecalciferol [24,25-(OH)2D3] had no effect on proliferation, DNA synthesis, or GAG synthesis of growth cartilage cells in the logarithmic growth phase. However, 24,25-(OH)2D3 had no effect on DNA synthesis of these cells in confluent cultures, but stimulated their expression of the cartilage phenotype. The stimulatory effect was dose dependent and maximal at 10(-7) M. Since chondrocytes express their differentiated phenotype as they become confluent in culture, these results suggest that 1,25-(OH)2D3 stimulates the growth of rapidly proliferating chondrocytes with a poorly differentiated phenotype and suppresses their expression of the cartilage phenotype, while 24,25-(OH)2D3 stimulates expression of the differentiated phenotype of highly differentiated chondrocytes.

24,25-Dihydroxyvitamin D 3↗
PubMedDate not supplied

[Effect of vitamin D3 and its metabolites 1,25-dihydroxycholecalciferol and 24,25-dihydroxycholecalciferol on callus mineralization in rats with femoral fracture].

Additional administration of vitamin D3 at a physiological dose of 0.25 microgram daily into rats with femur fracture within 4 weeks did not affect the specific weight and chemical composition (content of Ca2+, P) in diaphyses of intact and impaired femurs as well as the content of Ca2+. Pi and activity of alkaline phosphatase in blood serum of the animals. At a higher dose 2.5 microgram daily vitamin D3 increased concentration of Pi in blood serum but did not alter the other parameters studied. Physiological doses of 1,25-dihydroxycholecalciferol (1.25 (OH)2D3) and 24,25-dihydroxycholecalciferol (24,25 (OH)2D3) (00.3 microgram and 0.25 microgram daily, respectively) did not affect the specific weight and composition of the impaired diaphyses, content of Ca2+ and activity of alkaline phosphatase in blood but increased slightly the Pi concentration. After a 5-fold increase in the dose of 1,25(OH)2D3 (0.15 microgram daily) specific weight and content of Ca2+ were decreased in the impaired bones with simultaneous increase in concentration of Ca2+, Pi and activity of alkaline phosphatase in blood serum. These data suggest that reparation was impaired under the conditions of acceleration of the bone tissue resorption. Increased doses of 24, 25(OH)2D3 (1.25 micrograms daily) stimulated the increase in specific weight and mineralization of the impaired bones and normalized the increased alkaline phosphatase activity in blood serum. Clinical examination of 24,25(OH)2D3 could be recommended as a drug stimulating the reparation under conditions of bone fracture.

24,25-Dihydroxyvitamin D 3↗
PubMed1982

[Effect of 1,25-dihydroxycholecalciferol and 24,25-dihydroxycholecalciferol on thyroid calcitonin content in the suckling or weanling rat].

We have examined the effects of vitamin D3 metabolites on plasma calcium, plasma calcitonin (CT) and thyroidal CT contents in Rats before and after weaning. A daily injection of 1,25-dihydroxycholecalciferol [1,25-(OH)2D3; approximately 25 pmoles/Rat/day during 4 days] induced a marked rise in plasma calcium (16.1 +/- 0.2 vs. 11.3 +/- 0.3 mg/dl in controls) and a great decrease in thyroidal CT content (-70% of control values) in 13-day-old suckling baby Rats, while no change occurred in response to 24,25-dihydroxycholecalciferol (24,25-(OH)2D3) administration. A negative correlation between plasma calcium level and thyroidal CT stores was found in suckling and in weaning Rats treated with different doses of 1,25-(OH)2D3. The significant difference between the slopes of the two regression lines demonstrated a greater mobilization of the CT stores in weaning than in suckling Rats in response to a given hypercalcemia. Our results could suggest that 24,25-(OH)2D3 at the dose used, does not regulate CT secretion while 1,25-(OH)2D3 has probably an indirect effect on CT release, but in vitro experiments will be performed to confirm this hypothesis.

24,25-Dihydroxyvitamin D 3↗
PubMed1994

Synthesis of and response to 1,25 dihydroxycholecalciferol by subpopulations of murine epidermal keratinocytes: existence of a paracrine system for 1,25 dihydroxycholecalciferol.

The epidermis is both a target tissue for and a source of 1,25 dihydroxycholecalciferol. The present study determines which of the epidermal cell populations synthesizes 1,25 dihydroxycholecalciferol and which responds to this hormone. Epidermal keratinocytes from new born rat epidermis were separated by unit gravity sedimentation into poorly differentiated cells, slow-cycling more differentiated cells, actively proliferating cells, and terminally differentiating subpopulations. The keratinocyte populations were characterized by cell size analysis, cell morphology, and DNA and RNA contents (acridine orange flow cytometry). 1,25(OH)2D3 synthesis was studied by measuring the conversion of [3H] 25(OH)D3 to [3H] 1,25(OH)2D3. The purified product was tested for its ability to compete with synthetic [3H] 1,25(OH)2D3 for binding to chick intestinal cytosol. The responses of the keratinocyte subpopulations to exogenous 1,25(OH)2D3 were evaluated by the increase in 25(OH)D3-24 hydroxylase activity. Furthermore the expression of 1,25(OH)2D3 receptors (VDR) was examined in these cell populations. The results show that only the least differentiated cells produced 1,25(OH)2D3. In contrast, immunocytochemical detection of VDR, the VDR mRNA, and a 25(OH)D3-24 hydroxylase response to 1,25(OH)2D3 were mainly found in the more differentiated cells. Thus, the ability of epidermis to synthesize 1,25(OH)2D3 and be simultaneously sensitive to it depends on the state of cell differentiation. This suggests that the mammalian epidermis contains a paracrine system in which the more differentiated keratinocytes are sensitive to the 1,25(OH)2D3 produced locally by neighboring immature ones.

Animals↗
PubMed1982

Some characteristics of cytosol binding protein for 1 alpha,25-dihydroxycholecalciferol, 24R,25-dihydroxycholecalciferol and 25-hydroxycholecalciferol in rat parotid gland.

1. 1 alpha,25-dihydroxycholecalciferol (1,25-(OH)2VD3), 24R,25-dihydroxycholecalciferol (24,25-(OH)2VD3) and 25-hydroxycholecalciferol (25-OHVD3) binding proteins were existed in cytosol of rat parotid gland. 2. The dissociation constants of binding proteins for 1,25-(OH)2VD3, 24,25-(OH)2VD3 and 25-OHVD3 were 3.15 x 10(-9), 5.05 x 10(-9) and 6.60 x 10(9) M, respectively. 3. The mol wt and the isoelectric point (pI) of binding proteins for 1,25-(OH)2VD3, 24,25-(OH)2VD3, 24,25-(OH)2VD3 and 25-OHVD3 were the same to each other (with mol wt of 155,000 and pI of 4.87). 4. The binding specificity of 1,25-(OH)2VD3 binding protein was similar to that of 24,25-(OH)2VD3 and 25-OHVD3 binding protein. 5. The extent of loss of binding activity for 1,25-(OH)2VD3 by pronase and trypsin was much greater than that of binding activity for 24,25-(OH)2VD3 and 25-OHVD3.

Animals↗