Affinity chromatographic purification of serum retinol-binding protein using 4-substituted aminoretinoids.
Retinol-binding protein has been purified from rabbit serum by a new affinity chromatographic phase. Human retinol-binding protein has been shown to bind with vitamin A derivatives and certain other terpenoids. Consequently, this affinity method is based upon the ability of the protein to reversibly bind to beta-ionone and employs a derivatized affinity ligand while preserving the integrity of the beta-ionone molecule via substitution of the allylic 4-position. Purification is relatively simple when compared with other known methods and the yield from serum is similar to other schemes. The protein is obtained in the apo-form and retains the ability of the native protein to bind retinol.
Chapman
J M
JM
Division of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, Ohio State University, Columbus 43210.
Curley
R W
RW
D000818:Animals; D001059:Apoproteins / Q000302:isolation & purification; D002846:Chromatography, Affinity / Q000379:methods; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D013058:Mass Spectrometry; D008970:Molecular Weight; D011817:Rabbits; D012176:Retinoids / Q000138:chemical synthesis*; D012177:Retinol-Binding Proteins / Q000302:isolation & purification*
D001059:Apoproteins; D007202:Indicators and Reagents; D012176:Retinoids; D012177:Retinol-Binding Proteins