Perhaps the most common and powerful analytical technique being used for the analysis of biomolecules is high-performance liquid chromatography (HPLC). With the recent integration of biotechnology into numerous aspects of biochemistry and chemistry, HPLC specifically, reversed-phase liquid chromatography is playing an increasingly more important role in the purification and characterization of proteins. Through this project, two HPLC systems are being purchased to be used primarily in the advanced undergraduate biochemistry and chemistry laboratories. They are also being made available both for use in the instrumental analysis class and for undergraduate independent study projects. The HPLC systems are being used in the biochemistry laboratory in conjunction with capillary electrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis to analyze cell extracts and purified protein from E. coli lines that overproduce a recombinant protein. Generally, students in undergraduate laboratories are provided with a single method to illustrate a particular type of analysis. Rarely are they asked to directly compare methods to determine the relative strengths and weaknesses of each method. The new units are being used in the undergraduate chemistry laboratory to evaluate the effect of varying the flow-rate and gradient profile on the elution patterns of a series of proteins. Students are examining from a theoretical and practical point of view, special considerations and difficulties encountered by the analytical chemist dealing with biological systems. *
