Abstract
The cofactor of lactate oxidase from pneumococci is flavin mononucleotide (FMN). The apoenzyme of lactate oxidase is specifically activated by FMN. This chapter discusses a method for the enzymatic determination of FMN that depends on this activation. This method is similar to the determination of flavin adenine dinucleotide (FAD) with D-amino acid apo-oxidase and is applied in biochemistry. The chapter reviews the principle, the equipment, and the reagents used in the method. The activity of lactate oxidase is proportional to the amount of FMN within certain limits; it is determined manometrically by the oxygen uptake per unit time. A standard curve is obtained if the reaction rates with known concentrations of FMN are plotted against the FMN concentration. The chapter further highlights the preparation of solutions for the method and the stability of these solutions. FMN can also be determined spectrophotometrically by means of its activation of the apoenzyme of NADPH cytochrome c reductase.
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