Riboflavin Binding Protein (RBP) is a stable glycophosphoprotein abundant in the eggs of many oviparous species, including chickens. The function of the protein is to transfer riboflavin (Rf) to the developing embryo, and recent evidence suggests it also binds copper. Because of its bright yellow color and fluorescence, Rf transport serves as an excellent model system. A natural mutant strain of white leghorn chickens, containing a site mutation, is unable to synthesize RBP and thus the eggs are devoid of Riboflavin. We are currently investigating the protein and mutant egg use for both an undergraduate biochemistry lab (1) as well as an outreach project for K-12 students (2). The undergraduate research-style experiment for advanced biochemistry lab students is a useful exercise in learning protein purification techniques, including dialysis, salt precipitation and chromatography. Because of the holoRBP yellow color, it is easy to follow, and its stability renders it possible to carry out steps over time at room temperature. We have modified a standard procedure and students have successfully purified protein. Using the mutant and regular chicken eggs we have modified an education series as an informative and didactic approach towards problem-based learning. Our main motive was to perform outreach to K-12 with an interactive experiment featuring the importance of vitamins and the mechanisms of molecular transport.
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