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- W79137939 abstract "The authors have characterized and partially purified an enterocyte cytosolic 25 hydroxyvitamin D (250HD) binding protein which may participate in transcellular vitamin D metabolite transport. Triglyceride-rich emulsion particles (1%/wt/vol) containing /sup 3/H-250HD were incubated with rat intestinal cytosol or buffer for 0.5 hr. The reaction mixture was rapidly cooled and the mixture was centrifuged at 65,000g for 1 hr. Aliquots of buffer or cytosol infranatant were taken for scintillation counting. Only 4% of /sup 3/H-250HD transferred from the emulsion particles to buffer whereas 29% transferred to cytosol. Fractionation of cytosol by ammonium sulfate precipitation showed that the 60-80% saturation cut contained the 250HD binding activity. When this ammonium sulfate fraction was labeled with /sup 3/H-250HD and then subjected to gel permeation HPLC using a Toyo Soda G3000SW column, the /sup 3/H-250HD eluted in association with a peak of protein of MW/sup app/=68,000. The protein bound /sup 3/H-250HD eluted as a single peak on DEAE Sephacel anion exchange chromatography. The cytosolic 250HD binding activity was totally inactivated by heating to 60/sup 0/C for 1 hr. Serum vitamin D binding protein (sDBP) is stable under these heating conditions and has a MW/sup app/=58,000. They conclude that rat intestinal cytosol contains a 250HDmore » binding protein whose MW and heat stability characteristics indicate that the cytosolic protein is distinct from sDBP.« less" @default.
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- W79137939 date "1986-01-01" @default.
- W79137939 modified "2023-09-24" @default.
- W79137939 title "Partial purification of cytosolic 25 hydroxyvitamin D binding protein from rate enterocytes" @default.
- W79137939 hasPublicationYear "1986" @default.
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