Publication Date:
1980-09-12
Description:
Specific binding of 1 alpha,25-dihydroxyvitamin D(3) was found in nuclear and cytosol fractions of the bovine pituitary. For nuclear binding. the dissociation constant was 0.1 namomole per liter, and maximum binding was 104 femtomoles per milligram of protein. In competition studies, 25-hydroxyvitamin D(3) was 300 times weaker than 1 alpha,25-dihydroxyvitamin D(3). The existence of high-affinity sites supports a physiologic role for 1 alpha,25-dihydroxyvitamin D(3) in the pituitary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gelbard, H A -- Stern, P H -- U'Prichard, D C -- New York, N.Y. -- Science. 1980 Sep 12;209(4462):1247-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6250221" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Brain/metabolism
;
Cattle
;
Cell Nucleus/metabolism
;
Cholecalciferol/*metabolism
;
Cytosol/metabolism
;
Dihydroxycholecalciferols/*metabolism
;
Hydroxycholecalciferols/*metabolism
;
Kinetics
;
Pituitary Gland/*metabolism/ultrastructure
;
Receptors, Drug/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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