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The Characterization of Recombinant Riboflavin Binding Protein
Author(s) -
Jones Robert T,
Smith Sheila R,
Benore Marilee
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.894.5
Subject(s) - recombinant dna , histidine , chemistry , riboflavin , yolk , copper , binding site , biochemistry , plasma protein binding , microbiology and biotechnology , gene , biology , enzyme , food science , organic chemistry
Riboflavin Binding Protein (RBP) is a phosphoglycoprotein that is responsible for binding and delivery of riboflavin during embryonic development in hens. There are three forms of RBP: serum RBP (sRBP), yolk RBP (yRBP) and albumen RBP (wRBP) made from one gene. RBP binds copper in vitro in a 1:1 ratio, and the elucidation of the binding site would be of significance. Previous evidence suggests copper binding is at a Histidine residue. The goal of this study was to create and characterize recombinant plasmids of RBP in order to determine if His is required for copper binding. This work is supported by a grant from the University of MI at Dearborn.