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- W966884575 abstract "This chapter describes the purification of glutamate synthase from E. coli and K. aerogenes. These glutamate synthases are active with NADPH. The isolation of glutamate synthase from the eucaryote Saccharomyces cerevisiae is also described. This glutamate synthase uses only NADH. The purification procedure of glutamate synthase from K. aerogenes (or E. coli) consists of several steps including sonication, heat denaturation of impurities, protamine sulfate precipitation, ammonium sulfate precipitation, and gel filtration on Sephadex G-50. All the steps are carried out at 4° and the centrifugations are done at 16,000 g for 30 minutes. This procedure is also suitable for the purification of glutamate synthase from E. coli B. The purified enzyme gives a single band on polyacrylamide gel electrophoresis in 0.1 M Tris-acetate (pH 8.0). It exhibits a symmetrical boundary in sedimentation velocity runs in the analytical ultracentrifuge." @default.
- W966884575 created "2016-06-24" @default.
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- W966884575 date "1985-01-01" @default.
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- W966884575 title "[42] Glutamate synthase from Escherichia coli, Klebsiella aerogenes, and Saccharomyces cerevisiae" @default.
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- W966884575 doi "https://doi.org/10.1016/s0076-6879(85)13045-4" @default.
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