Assimilatory nitrate reductase and glutamate dehydrogenase of the red alga Porphyridium aerugineum have been studied. Nitrate reductase exhibits a pH optimum at approx. 7.75; it is functional with reduced benzyl viologen, FMN; FAD, NADH and is not functional with NADPH. In crude extracts of cells grown on nitrate as the sole nitrogen source, a partially inactive form of nitrate reductase occurs. This inactive enzyme can be activated by heating at 50°C. Glutamate dehydrogenase of P. aerugineum is strictly dependent on NADPH. © 1979.
Nitrate reductase and glutamate dehydrogenase of the red alga Porphyridium aerugineum
FUGGI, Amodio
1979
Abstract
Assimilatory nitrate reductase and glutamate dehydrogenase of the red alga Porphyridium aerugineum have been studied. Nitrate reductase exhibits a pH optimum at approx. 7.75; it is functional with reduced benzyl viologen, FMN; FAD, NADH and is not functional with NADPH. In crude extracts of cells grown on nitrate as the sole nitrogen source, a partially inactive form of nitrate reductase occurs. This inactive enzyme can be activated by heating at 50°C. Glutamate dehydrogenase of P. aerugineum is strictly dependent on NADPH. © 1979.File in questo prodotto:
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