Eggs, vitamins, color, and fluorescence all play a part in this classroom demonstration by Prof. Hal White of the University of Delaware. The demonstration i...

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Comment by Dr Henry Furneaux on June 3, 2013 at 1:17pm

yup, indeed , lots of potential , I will be trying it out in the fall semester !

Will let you know what happens !

best

Henry

Comment by Harold B. White on June 3, 2013 at 1:08pm

Henry,Approaching this from a nuitional perspective works well. Chick embryos and humans need similar nutrients to grow and survive. The great feature of riboflavin is that you can actually see the vitamin in normal egg white. In the absence of mutant eggs, you could show normal eggs and then tell the story about eggs that have clear colorless egg whites and don't hatch and have students propose explanations.

Hal

Comment by Dr Henry Furneaux on June 3, 2013 at 11:20am

Hi . Many thanks for the rapid  feedback.  I was thinking of presenting the biology first , these eggs develop , these do not . Then asking the students to figure it out ( with a little prompting) . So they would want to look in the egg and would discover the  difference.  I would forsee that several lab exercises would be needed to answer the question .   If the eggs  are not readily available , I could  provide egg white . Using affinity chromatography , i could create egg white that lack riboflavin and that lacks the binding protein and would be a mimic.

Providing  them with the sequence of the w.t. and mutant genes  might be a great way for them to discover splicing !

Thanks for your help

best

Henry

Comment by Harold B. White on June 3, 2013 at 11:08am

Henry,

I no longer do research on the riboflavin-deficient strain of chickens and it is no longer maintained here at the University of Delaware. Marilee Benore at the University of Michigan Dearborn, may be able to get you some eggs. The riboflavin-binding protein-deficiency in eggs is caused by a splicing mutation that results in a null allele, no protein is produced. [J. Biol. Chem. 268, 23222-23226 (1993)] The wild type protein is very easy to purify from chicken egg white where it constitutes about 0.5% of the protein and binds very strongly to DEAE cellulose. [Meth. Enzymol. 122, 227-234 (1986)] Details of the demonstration have been published. [ J. Chem. Educ. 65, 814-815 (1988)] and a laboratory experiment for a biochemistry course has been published [J. Chem. Ed. 67, 803-804 (1990)].   I doubt that a recombinant protein is available or would be desirable since there are a number of post-translational modifications to the protein. [Ann. Rev. Nutr. 8, 279-299 (1988)]

While the demonstration is great with a supply of eggs from mutant hens, that is icing on the cake. Because the demonstration involves familiar things--eggs, vitamins, color, and fluorescence, it can be easily modified and retain student interest. For a little twist, you might want to include duck eggs which have the riboflavin-binding protein in their egg white, but there is no yellow color because there is virtually no riboflavin present. The demonstration works best in a totally darkened room and a good UV light source.

Good luck.

Hal White

Comment by Dr Henry Furneaux on June 3, 2013 at 9:46am

 I want to  do  this.

Where can you get  the  eggs that lack the binding protein ?

What's the mutation  ?

 (mutation in regulatory region or  deletion?   or is it an amino acid change in protein ) ?

Is purified (or recombinant )  binding protein available ? This would enable adding it  back    to restore quenching .

Presumably it can be purified using a riboflavin  affinity column ?

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