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Identification of the ammonium‐dependent isoenzyme of glutamate dehydrogenase as the form induced by senescence or darkness stress in the first leaf of wheat
Author(s) -
Laurière C.,
Daussant J.
Publication year - 1983
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1983.tb04148.x
Subject(s) - glutamate dehydrogenase , darkness , isozyme , senescence , ammonia , ammonium , glutamine synthetase , biochemistry , biology , glutamate synthase , glutamate receptor , incubation , enzyme , chemistry , glutamine , amino acid , botany , microbiology and biotechnology , receptor , organic chemistry
The level of glutamate dehydrogenase activity increases nearly 3 fold in detached wheat ( Triticum aestivum L. cv. Capitole) leaves during 72 h incubation with 15 mM ammonia. De novo synthesis of one of the glutamate dehydrogenase isoenzymes is shown to be correlated with the activity increase, by using an immunochemical approach. The identification of the ammonia inducible isoenzyme as the form previously reported induced by darkness stress or senescence (Laurière et al. 1981, Physiol. Plant. 52: 151‐155), provides new information on the possible physiological significance of the response to ammonia.