Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10574204 | Journal of Inorganic Biochemistry | 2006 | 4 Pages |
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
Authors
Sheila R. Smith, Irina Pala, Marilee Benore-Parsons,