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

Authors

Manu ChakravarthyFollow
Laura Snyder
Timothy Vanyo
Jill Holbrook
Henry V. Jakubowski, College of Saint Benedict/Saint John's UniversityFollow

Document Type

Article

Publication Date

3-1996

Disciplines

Biochemistry | Biochemistry, Biophysics, and Structural Biology | Chemistry | Curriculum and Instruction | Education | Higher Education | Life Sciences | Physical Sciences and Mathematics

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.

Comments

DOI: 10.1021/ed073p268

Recommended Citation

Chakravarthy, M.; Snyder, L.; Vanyo, T.; Holbrook, J.; Jakubowski, H. V. Protein Structure and Chromatographic Behavior: The Separation and Characterization of Four Proteins Using Gel Filtration and Ion-Exchange Chromatography and Gel Electrophoresis. J. Chem. Educ., 1996, 73(3), 268-272.