University of MI at Dearborn, Natural Sciences, Dearborn, MI 48128
Riboflavin Binding Protein (RBP) is a hen glyco-phospho-protein that transports the nutrient riboflavin to the oviduct and oocyte. Recent work in our labs indicates the protein also binds copper in a 1:1 ratio. The site of copper binding to Riboflavin Binding Protein is unclear, although it appears his residues are involved. We are interested in determining if the phosphoserine residues participate in copper binding. It is possible, though unlikely that the metal binds to one of the numerous phosphoserine residues or that the phosphoserine residues alter the binding affinity or ratio. RBP was dephosphorylated, dialyzed against copper, and the copper binding characterized using Atomic Absorption Spectroscopy.
[Abstract (DOC)]