PLANT PHYSIOLOGY · 1982 · 97 citations · 26 references
Life SciencesPlant BiologyPlant SciencesPlant BiochemistryPlant Molecular BiologyPlant PhysiologyAntioxidant DefensePlant EnzymesEnzymesGlutamate DehydrogenaseRoot Tissues
Rabbit antiserum was raised against ferredoxin-dependent glutamate synthase (EC 1.4.7.1) purified from green leaves of Oryza sativa L. cv Delta. Ferredoxin-dependent glutamate synthase, detected in green leaf, etiolated leaf, and root tissues cross-reacted completely with the antiferredoxin glutamate synthase immunoglobulin G. In contrast, the immunoglobulin G did not cross-react with NADH-dependent (EC 1.4.1.14) and NADPH-dependent (EC 1.4.1.13) glutamate synthases found in nonphotosynthetic etiolated leaf and root tissues. In addition, ferredoxin-dependent glutamate synthase was separated and distinguished by its affinity to ferredoxin from NAD(P)H-dependent glutamate synthase on ferredoxin-Sepharose affinity chromatography. Based on the immunological studies, it is suggested that ferredoxin-dependent glutamate synthases in green leaf and etiolated leaf tissues are closely related proteins; in contrast, ferredoxin-dependent glutamate synthase in root tissue is a distinct protein from the leaf enzymes.
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Measurement of protein by spectrophotometry at 205 nm
R.K. Scopes · Analytical Biochemistry · 1974 · 764 citations
Alternative route for nitrogen assimilation in higher plants
Peter J. Lea, B. J. Miflin · Nature · 1974 · 563 citations
The pathway of nitrogen assimilation in plants
Benjamin J. Miflin, Peter J. Lea · Phytochemistry · 1976 · 537 citations