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- W2027234922 abstract "A daily rhythm in the activity of nitrate reductase (NR: EC 1.6.6.1) isolated from the marine red algae Gracilaria tenuistipitata is shown to be attributable to changes in amounts of the protein. The enzyme was purified in four steps: ion exchange Q-Sepharose separation, ammonium sulfate precipitation, gel filtration on Sephacryl S-300, and affinity chromatography on Affigel-blue resin. This purification procedure yielded an active purified NR of about 500-fold with a recovery of 85%. The SDS–PAGE silver staining of purified NR revealed a 110 kDa single band. Non-denaturated protein showed a molecular mass of 440 kDa on gel filtration comparing with SDS–PAGE, the enzyme is apparently composed of four identical subunits. In extracts of algae grown under either constant dim light or a light–dark cycle, the activity of NR exhibited a daily rhythm, peaking at midday phase as does photosynthesis. Staining with monoclonal antibodies, raised against NR from Porphyra yezoensis, showed that the amount of protein changes by a factor of about 12, with a maximum occurring in the midday phase." @default.
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- W2027234922 date "2002-07-01" @default.
- W2027234922 modified "2023-10-01" @default.
- W2027234922 title "Characterization and daily variation of nitrate reductase in Gracilaria tenuistipitata (Rhodophyta)" @default.
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- W2027234922 doi "https://doi.org/10.1016/s0006-291x(02)00621-6" @default.
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