Induction of resting cells ofPseudomonas natriegens, nov. spec. to the oxidation of L-arabinose and mannitol, and an additional marine isolate (L5) to oxidation of lactose and mannitol, was found dependent on the presence of Na+ with marine levels of Mg++ and K+ included in the suspending media. However, omission of Na+ and Mg++, and increase of the concentration of K+ in the suspending media, permitted rapid utilization of these substrates (but not of glucuronate) by resting cells and greatly accelerated the rates of induced enzyme formation. Inclusion of Mg++ in the suspending media suppressed the rates of induction and oxidation stimulated by elevation of the K+ concentration. Incubation of resting cells of isolate L5 in an assay medium containing 0.26 M KCl preserved the ability of the organisms to produce a significant level of the enzymes for oxidation of mannitol, even after 8 hrs aging of the cells in the cold. Chloramphenicol inhibited the synthesis of induced oxidative enzymes in both these marine isolates suspended in high K+ medium, and the extent of inhibition was proportional to the time of addition of the antibiotic. Interruption of induction of isolate L5 cells to mannitol by washing within 30 min removed the stimulatory effect of the elevated level of K+, whereas longer periods of incubation before interruption yielded cells more fully induced. A greater amount of β-galactosidase was produced by resting cells of the marine isolate L5 incubated with the inducer in media with elevated K+ concentrations than by those cultured on lactose or induced in the resting state in the presence of Na+. Moreover, inclusion of an elevated K+ concentration in the suspending media stimulated the production of L-arabinose isomerase in resting cells ofP. natriegens. The requirement for Na+ for the growth of these bacteria, however, was not replaceable by elevation of the K+ concentration of culture media.