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The Purification of Horse Heart Cytochrome c by Ion Exchange Chromatography

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Patricia Ann Mabrouk

Department of Chemistry, Northeastern University, Boston, MA 02115

J. Chem. Educ., 1996, 73 (7), p A149

DOI: 10.1021/ed073pA149

Publication Date (Web): July 1, 1996

Abstract

While enormous changes have occurred in the past decade in the field of analytical chemistry, the curriculum for undergraduate Quantitative Analysis has changed very little. This paper describes a highly successful experiential learning laboratory experiment for use in undergraduate Quantitative Analysis which capitalizes on current student interest in biotechnology. In the multi-week experiment, students investigate the preparative scale purification of horse cytochrome c by ion exchange chromatography using a two-wavelength UV-vis purity assay to characterize the chromatographed protein. The experiment emphasizes critical thinking and allows students to assimilate and apply the fundamental concepts underlying separations (dialysis; ion exchange), acid-base (buffers), UV-vis spectrophotometry, and redox (oxidants/reductants) chemistry. Remarkably, while most students consider the experiment to be extremely difficult, 55% rank this experiment as the best experiment in our current quantitative analysis laboratory curriculum.