Fefolding of pyridoxine-5'-P oxidase assisted by GroEL

摘要

The unfolding of brain pyridoxine-5'-P oxidase by guanidinium chloride has been investigated at equilibrium. Circular dichroism, fluorescence spectroscopy and gel exclusion chromatography were used to monitor the unfolding process. the enzyme dissociates reversibly into monomers, but the fluorescence properties of the cofactor FMN are not restored upon dilution with potassium phosphate buffer(pH 7.4). spontaneous refolding leads to 20/100 recovery of the catalytic activity.