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Abstract: Expressing and Purifying Soybean Lipoxygenase in Escherichia coli
Author: Babette Burcaw
Faculty Advisor: Ted Holman, Assistant Professor of Chemistry
With: Eric Johansen, Staff Research Associate


The enyzyme Lipoxygenase catalyzes the first step in the metabolism of arachidonic acid and leads to the formation of the physiological effectors: leukotrines and lipoxins. These agents cause broncho-constriction and vaso-constriction as well as other phsiological effects, including tumor cell metastasis.

To better understand its structure, function, and chemical mechanism, lipoxygenase enzyme from soybeans, whose substrate is linoleic acid, was used in this expression and purification process.

The enzyme was expressed using an E. coli expression system and then subjected to purification via column chromatography. After obtaining the purified product, enzyme kinetics and activity assays were performed to characterize the properties of the enzyme. By better understanding the properties of the enzyme, the development of lipoxygenase inhibitors could thus lead to medications indicated for the treatment of asthma and other inflammatory diseases.

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