Article ID Journal Published Year Pages File Type
10574204 Journal of Inorganic Biochemistry 2006 4 Pages PDF
Abstract
Riboflavin binding protein, purified from egg white, binds copper(II) under dialysis conditions in an approximately 1:1 molar ratio. Results further indicate a small, but not negligible, amount of copper is present in the protein as purified from egg white. Electron paramagnetic resonance indicates a single type II copper site present in the protein. These results suggest the possibility of a previously unknown function of riboflavin binding protein in the storage or transport of copper.
Related Topics
Physical Sciences and Engineering Chemistry Inorganic Chemistry
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