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- W2039244872 abstract "The NADPH–glutamate dehydrogenase (GDH; EC 1.4.1.4) from glutamate–grown cells of Euglena gracilis Klebs strain z. Pringsheim was purified to homogeneity by the criterion of polyacrylamide gel electrophoresis. The holoenzyme was shown to have a relative molecular mass of 180000 and to be composed of four subunits with a relative molecular mass of 45000. The pH optimum for the animating reaction was 80. The Km values for NH4+, α-oxoglutarate and NADPH were 0.4 mM, 1.4 mM and 0.18 mM, respectively. Antibodies raised to the purified enzyme showed no immunological correspondence with glutamic dehydrogenases from nitrate–grown Stichococus bacillaris and Porphyridium cruentum or ammonium–grown Chlorella vulgaris on Ouchterlony double–diffusion gels or by immuno–precipitation of enzyme activity. It is concluded that antigenic sites on the tetrameric Euglena enzyme may not be available on other NADPH–GDHs if they are hexamers." @default.
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- W2039244872 date "1986-11-01" @default.
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- W2039244872 title "PROPERTIES AND IMMUNOCHEMICAL CHARACTERIZATION OF NADPH-SPECIFIC GLUTAMATEDEHYDROGENASE FROM EUGLENA GRACILIS" @default.
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- W2039244872 doi "https://doi.org/10.1111/j.1469-8137.1986.tb02908.x" @default.
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