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Some characteristics of new tissue-binding proteins for metabolites of vitamin D other than 1,25-dihydroxyvitamin D
Authors:DEM Lawson  Marilyn Charman  PW Wilson  S Edelstein  
Institution:University of Cambridge and Medical Research Council, M.R.C. Dunn Nutrition Unit, Milton Road, Cambridge, CB4 1XJ U.K.
Abstract:Protein(s) have been found in a wide range of tissues which have a high affinity for 25-hydroxycholecalciferol. Of the tissues examined only erythrocytes do not have this protein. The properties of the protein have been examined and it has been found that the association constants range from 2 · 109 to 5 · 109 M−1 and the sedimentation constants between 5.0 and 6.0 S. It was not possible to distinguish the proteins from the different tissues by their S values, mobility on gel electrophoresis or behaviour on ion-exchange chromatography. These techniques were all used, however, to show that the tissue 25-hydroxycholecalciferol binding protein is distinct from the main plasma binding protein for this steroid and from the intestinal 1,25-dihydroxycholecalciferol-binding protein. A protein has been found in the plasma of rachitic animals but not of normals, which is apparently indistinguishable from this new tissue 25-hydroxycholecalciferol-binding protein. The steroid specificity of this new binding protein has been shown to be dependent upon a C-25 hydroxyl group, and an intact conjugated double bond system. Possible functions for this protein have been briefly discussed.
Keywords:cortisol  11β  17  21-trihydroxypregn-4-ene-3  20-dione  cortexolone  17  21- dihydroxypregn-4-ene-3  20-dione  dexamethasone  9α-fluoro-16α-methyl-11β  17  21-trihydroxy- pregna-1  4-diene-3  20-diene  triamcinolone acetonide  11β  21-dihydroxy-9α-fluoropregna-1  4- diene-3  20-dione-16α  17α-acetonide
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