Abstract
Human serum binding protein for vitamin D and its metabolites. I. Physicochemical and immunological identification in human tissues.
Highlights
The physicochemical and immunological characteristics of the human tissue binding protein for 25-hydroxycholecalciferol (25-OH-D3) were studied
On sucrose gradients (Fig. 2), iodinated DBP co-sedimented with 25OHj3H]D3 bound to serum, and both were less dense than the bovine serum albumin marker
As reported previously for rat muscle [15], the 25-OH-r3H]D3 bound by human skeletal muscle cytosol sedimented in the 5 to 6 S region, faster than bovine serum albumin
Summary
The physicochemical and immunological characteristics of the human tissue binding protein for 25-hydroxycholecalciferol (25-OH-D3) were studied. The ‘251-labeled complex was dissociated by 6 M guanidine HCl or sodium dodecyl sulfate (SDS) treatment, resulting in “‘1 sucrose gradient sedimentation and SDS-polyacrylamide gel electrophoresis migration characteristic of the serum binding protein. These data provide clear evidence that the tissue binding protein represents an interionic association between an unidentified tissue factor and the serum binding protein. Human serum DBP has been isolated and partially characterized in several laboratories (l-3) It is a 3.5 S, M, = 58,000 single polypeptide chain which has a binding preference for 25-OH-D3 over vitamin D3 and 1,25-
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