Interaction of vitamin D-binding protein with immobilized cibacron blue F3-GA.
An interaction of vitamin D-binding protein to immobilized Cibacron Blue F3-GA was studied under urea containing buffers. In these buffers, this protein was adsorbed to the immobilized dye and was eluted with salt gradients as in the same buffer without urea. The protein was also adsorbed to immobilized diethylaminoethyl but not to immobilized carboxymethyl. It is implicated that a combination of pseudo-ligand affinity and/or hydrogen bonding interaction plays a large role whereas ionic, hydrophobic and lipophilic interactions act little between the protein and the immobilized blue dye.
Egawa
T
T
Third Department of Internal Medicine, Osaka University Medical School, Japan.
Yamamoto
H
H
Nakamura
H
H
Kishimoto
S
S
D002021:Buffers; D002499:Centrifugation, Density Gradient; D002762:Cholecalciferol / Q000737:chemistry; D002852:Chromatography, Ion Exchange; D004396:Coloring Agents / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D014227:Triazines / Q000737:chemistry*; D014508:Urea / Q000737:chemistry; D014809:Vitamin D-Binding Protein / Q000737:chemistry*
D002021:Buffers; D004396:Coloring Agents; D014227:Triazines; D014809:Vitamin D-Binding Protein; D002762:Cholecalciferol; C012842:Cibacron Blue F 3GA; D014508:Urea