Abstract
Publisher Summary This chapter presents a procedure for the preparation of formaldehyde dehydrogenase. Formaldehyde dehydrogenase can be assayed by recording the initial velocity spectrophotometrically at 340 nm and 25°. Either the formation of nicotinamide adenine dinucleotide–hydrogen (NADH) in the forward reaction, or the disappearance of NADH in the reverse reaction can be measured. For crude tissue preparations, only the forward reaction assay may be used because of the presence of a large excess of activity catalyzing the hydrolysis of S -formylglutathione. The enzyme can be purified to homogeneity from the human liver, involving extraction; salt fractionation; washing on diethylaminoethyl (DEAE)-cellulose 1and DEAE-cellulose 2; isoelectric focusing; and finally washing on Sephadex G-100, hdroxylapatite, and QAE-Sephadex column. The final preparation is homogeneous in polyacrylamide electrophoresis under denaturing and nondenaturing conditions and represents about 1400-fold purification over the crude soluble fraction of the human liver.
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