EFFECT OF GROWTH CONDITIONS ON NADPH-SPECIFIC GLUTAMATE DEHYDROGENASE ACTIVITY OF EUGLENA GRACILIS.

Cells of Euglena gracilis Klebs, strain z Pringsheim, had high NADPH-glutamate dehydrogenase (GDH) activity when grown on glutamate but activity was repressed completely in cells grown on ammonium (NH ). Subcellular fractionation showed that NADPH-GDH activity was located exclusively in the cytosol, while glutamine synthetase was present in the cytosol and chloroplasts. Despite high NADPH-GDH activity NH assimilation was completely inhibited by methionine sulphoximine (MSO), an inhibitor of glutamine synthetase.

Glycollate-pathway enzymes in mitochondria from phototrophic, organotrophic and mixotrophic cells of Euglena.

Glycollate dehydrogenase and NADFH-glyoxylate reductase are constitutive enzymes in Percoll-purified mitochondria from phototrophic, mixotrophic and organotrophic cells of Euglena gracilis Klebs strain z Pringsheim. Glycollate oxidation by isolated mitochondria is stimulated four-fold by the addition of glutamate but rates of glycine oxidation are low in mitochondria from all cell types, the ratio of malate to glycine oxidation always being greater than 4:1. Measurement of the rate of NADPH oxidation in intact mitochondria and mitoplasts showed that the outer mitochondrial membrane is impermeable to NADPH and in the absence of NADPH-dehydrogenase activity the oxidation of NADPH by mitoplasts is dependent on the presence of glyoxylate for NADPH-glyoxylate-reductase activity.