Isolation and characterization of NADH-glutamate synthase from pea (Pisum sativum L.).

@article{Matoh1980IsolationAC,
  title={Isolation and characterization of NADH-glutamate synthase from pea (Pisum sativum L.).},
  author={Tōru Matoh and Shoji Ida and Etsuhisa Takahashi},
  journal={Plant & cell physiology},
  year={1980},
  volume={21 8},
  pages={1461-74}
}
Both ferredoxin-glutamate synthase (EC 1.4.7.1) and NADH-glutamate synthase (EC 1.4.1.14) were isolated separately on DEAE-cellulose chromatography from etiolated pea shoots. The latter enzyme was purified 1,400-fold by ammonium sulfate fractionation and column chromatographies of DEAE-cellulose, Sephadex G-200 and blue-Sepharose. The enzyme had a molecular weight of 220,000 and an isoelectric point of 4.3. The optimum pH was 7.6. Apparent Km values for l-glutamine, 2-oxoglutarate and NADH were… CONTINUE READING

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