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

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Timothy Vanyo , Jill Holbrook , Henry V. Jakubowski , Manu Chakravarthy and Laura Snyder

College of St. Benedict/St. John''s University, 37 South College Avenue, St. Joseph, MN 56374

J. Chem. Educ., 1996, 73 (3), p 268

DOI: 10.1021/ed073p268

Publication Date (Web): March 1, 1996

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.

Keywords (Domain):

Biochemistry

Keywords (Pedagogy):

Hands-On Learning / Manipulatives

Keywords (Subject):

Proteins / Peptides

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Received: August 03, 2009

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Article

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

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Recommend & Share

Related Content

Separation and Determination of Cr(III) and Cr(VI) with Cation-Exchange Chromatography and Atomic Absorption Spectroscopy. An Experiment for Quantitative Methods of Analysis

Collaboration between Chemistry and Biology to Introduce Spectroscopy, Electrophoresis, and Molecular Biology as Tools for Biochemistry

Digitally Enhanced Thin-Layer Chromatography: An Inexpensive, New Technique for Qualitative and Quantitative Analysis

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