Protein Structure and Chromatographic Behavior:: The Separation and Characterization of Four Proteins Using Gel Filtration and Ion-Exchange Chromatography and Gel Electrophoresis

• Timothy Vanyo ^[1] ; Jill Holbrook ^[1] ; Henry V. Jakubowski ^[1] ; Manu Chakravarthy ^[1] ; Laura Snyder ^[1]
  1. [1] College of St. Benedict/St. John''s University
• Localización: Journal of chemical education, ISSN 0021-9584, Vol. 73, Nº 3 (March), 1996, págs. 268-272
• Idioma: inglés
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• Resumen

  • 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.