Studies on Nitro-Reducing Enzymes of Swine Liver

Abstract

Liver homogenates were extracted at pH 6.5, fractionated by ammonium sulfate between 0.40 and 0.45 saturation, adsorbed on a DEAE-cellulose column at pH 7.8, eluted with 0.006 and 0.08 [image] Na citrate, successively, to obtain partially purified nitro-and nitrosoreductases. Both enzymes were most active at pH 7.8, required reduced diphosphopyridine nucleotide as H-donor, and heavy metal as cofactor. Nitroreductase required flavine adenine dinucleotide as an electron carrier.