Premium
Improved purification scheme for Riboflavin Binding Protein
Author(s) -
Milligan Michael,
Turner Geraldine,
Smith Sheila Rose,
Benore Marilee Ann
Publication year - 2011
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.25.1_supplement.928.7
Subject(s) - riboflavin , chemistry , protein purification , yolk , chromatography , fractionation , extraction (chemistry) , recombinant dna , biochemistry , food science , gene
Riboflavin Binding Protein (RBP) is a glycophosphoprotein found in the eggs of oviparous species. Responsible for transporting riboflavin for the developing embryo, RBP also binds copper, suggesting other potential functions for this protein. Because of its stability and functional assets, RBP has been employed for use in structure‐activity studies and other uses. RBP is abundant in chicken egg albumen and yolk and can be isolated from eggs as well as from recombinant sources; several purification methods have been reported in the literature. Most procedures require one or more steps requiring high salt, low pH, or organic solvent extraction. Improved purification procedures that minimize stringent steps would allow for faster isolation as well as retention of all structural features. We have made improvements to the procedure for isolation of RBP, including modifications to the fractionation and chromatographic steps in the protocol.