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Chick intestinal cytosol binding protein for 1,25-dihydroxyvitamin D/sub 3/: a study of analog binding

Journal Article · · Arch. Biochem. Biophys.; (United States)
The structural features of 1,25-dihydroxyvitamin D/sub 3/ that permit its high affinity binding to a 3.7 S protein from chick intestinal cytosol were determined in a series of binding and competition experiments analyzed by sucrose density gradient centrifugation. Optimal binding to the 3.7 S protein was achieved when both 1..cap alpha..- and 25-hydroxyls were present in the vitamin D/sub 3/ molecule. Modification of the side chain by the introduction of a methyl on C-24 and a double bond on C-22,23 (1,25-dihydroxyvitamin D/sub 2/) did not alter the binding of 1,25-dihydroxyvitamin D/sub 3/, but significantly diminished the binding of 25-hydroxyvitamin D/sub 3/. However, introduction of a hydroxyl on C-24 decreased the ability of either 1,25-dihydroxyvitamin D/sub 3/ or 25-hydroxyvitamin D/sub 3/ to compete, especially when the 24-hydroxyl was in the S configuration. These results reveal that the 3.7 S protein requires specific ligand structural features for binding and suggest that metabolite discrimination by the chick intestinal receptor system is likely located in the 3.7 S cytosol protein.
Research Organization:
Univ. of Wisconsin, Madison
OSTI ID:
7208234
Journal Information:
Arch. Biochem. Biophys.; (United States), Journal Name: Arch. Biochem. Biophys.; (United States) Vol. 179; ISSN ABBIA
Country of Publication:
United States
Language:
English