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  Home > JCE Print > Journal of Chemical Education > Issues > 1996  > March  >
Laboratory Experiments
Protein Structure and Chromatographic Behavior: The Separation and Characterization of Four Proteins Using Gel Filtration and Ion-Exchange Chromatography and Gel Electrophoresis
Manu Chakravarthy, Laura Snyder, Timothy Vanyo, Jill Holbrook, and Henry V. Jakubowski
College of St. Benedict/St. John's University, 37 South College Avenue, St. Joseph, MN 56374
Cover
March 1996
Vol. 73 No. 3
p. 268

Abstract
Protein separation and purification is a hallmark of most undergraduate biochemistry labs. Traditional procedures involve the chromatographic separations of a single protein from a homogenate. This laboratory exercise describes the separation of four proteins which have been covalently modified to be visible during the separations. The simultaneous purification of four proteins allows students to develop an understanding not only of chromatographic techniques, but also how the structure of proteins influence chromatographic behavior.
More Information
*  Citation
Chakravarthy, Manu; Snyder, Laura; Vanyo, Timothy; Holbrook, Jill; Jakubowski, Henry V. J. Chem. Educ. 1996 73 268.
*  Keywords
*  History
Created:
Last Updated:
9/23/1999
5/22/2006
  Home > JCE Print > Journal of Chemical Education > Issues > 1996 > March > Page 268


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