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White bands resulting from precipitation of dodecan-1-ol liberated by hydrolysis of sodium dodecyl sulfate and decan-5-ol released by hydrolysis of decan-5-yl sulfate produced zymograms of the primary and secondary alkylsulfatases fromPseudomonas C12 B. Gas-liquid chromatographic analyses of ether extracts of the precipitate-containing segments of the zymograms confirmed the identity of the alcohols which were not discerned in extracts of segments of the gels other than those containing precipitates. β-Galactosidase fromEscherichia coli was marked on zymograms by the liberation ofo -nitrophenol fromo -nitrophenyl-β-D-galactoside, and arylsulfatase fromPseudomonas C12 B was marked in gels by liberation ofp -nitrophenol fromp -nitrophenyl sulfate. Membrane-associated dissimilatory nitrate reductases from a nitrate respirer (Enterobacter aerogenes ) and a denitrifier (Pseudomonas perfectomarinus ) did not penetrate either 6.8 or 3% polyacrylamide gel but were demonstrable at the top of the gels. In the membrane-bound state, formate served as electron donor for nitrate reductase fromE. aerogenes , and reduced nicotinamide adenine dinucleotide (NADH) served as donor for nitrate reductase fromP. perfectomarinus . Both enzymes reduced nitrate at the expense of reduced benzyl viologen as well. Assimilatory nitrate reductase fromE. aerogenes moved easily into the 6.8% gels (Rf = 0.43 under the conditions of these experiments). The reduced dye served as electron donor for the assimilatory reductase, but formate and NADH did not. Incubation of the membrane-associated nitrate reductases with 2% Triton X-100 solubilized the enzymes and removed the capacity of formate and NADH to serve as electron donors. Both retained the ability to reduce nitrate at the expense of reduced benzyl viologen. The solubilized dissimilatory reductase fromE. aerogenes moved further in the gels (Rf = 0.49) than the soluble assimilatory reductase; the solubilized dissimilatory reductase from the denitrifier,P. perfectomarinus , moved further in the gels (Rf = 0.64) than either of the enzymes fromE. aerogenes .

Methods for Visualization of Enzymes in Polyacrylamide Gels