Lab_Report_#4 - Electrophoretic Separation of Erythrocyte...

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Electrophoretic Separation of Erythrocyte Membrane Proteins Jaime Figlan Hatham Shawqi Department of Physiology At Michigan State University Tuesday, February 12, 2008
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Abstract This experiment was intended to determine the molecular weights of Band III, Actin, and two Spectrins in a dog (Cheerio) and a goat’s (Curly’s) erythrocytes. The hypothesis was that Actin is the smallest protein with a molecular weight of around 42,000 daltons, Band III has a slightly larger weight around 100,000 daltons, and both Spectrins are the largest with molecular weights of approximately 200,000 and 220,000 daltons. The molecular weights of the membrane proteins were determined experimentally by performing and analyzing a sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cheerio’s and Curly’s erythrocytes were provided by the Midwest Animal Blood Services located in Stockbridge, Michigan. The results show that the experimental values of the molecular weights of the 4 proteins of interest are approximately equal to the predicted values of the hypothesis. The largest difference between the experimental value and the predicted value was seen in the Actin protein of both erythrocyte samples.
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Introduction Many proteins contained within or associated with the plasma membrane play important roles in allowing erythrocytes to deliver oxygen and remove carbon dioxide from its surrounding tissues. Band III, an integral membrane glycoprotein, exchanges
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This note was uploaded on 05/16/2008 for the course PSL 475 taught by Professor Hootman during the Spring '08 term at Michigan State University.

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Lab_Report_#4 - Electrophoretic Separation of Erythrocyte...

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