Title : Occurrence of glutamate dehydrogenase isoenzymes during growth of Oocystis alga.

Pub. Date : 1983 Jul

PMID : 18551483






7 Functional Relationships(s)
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1 Oocystis sp., a unicellular green alga, contained two glutamate dehydrogenase isoenzymes: one was specific for NADH and the other for NADPH. NADP glutamate dehydrogenase 1 Homo sapiens
2 Activity staining after gel electrophoresis indicated that one component in NADH-GDH was not specific for the cofactor and three components in NADPH-GDH. NADP glutamate dehydrogenase 1 Homo sapiens
3 Activity staining after gel electrophoresis indicated that one component in NADH-GDH was not specific for the cofactor and three components in NADPH-GDH. NADP glutamate dehydrogenase 1 Homo sapiens
4 There was a sharp increase in NADPH-GDH activity following the exhaustion of ammonia from the medium but NADH-GDH activity remained unchanged. NADP glutamate dehydrogenase 1 Homo sapiens
5 The NADPH-GDH activity at the outset increased exponentially with time in greenhouse culture but then decreased sharply accompanied by a rapid increase in biomass and nitrite concentration. NADP glutamate dehydrogenase 1 Homo sapiens
6 The K(m) values for ammonia in this algal GDH was high, while glutamate synthase activity was not detected; this suggests that Oocystis may adapt to conditions of ammonia limitation by producing large quantities of NADPH-GDH instead of using glutamate synthase pathway. NADP glutamate dehydrogenase 1 Homo sapiens
7 The K(m) values for ammonia in this algal GDH was high, while glutamate synthase activity was not detected; this suggests that Oocystis may adapt to conditions of ammonia limitation by producing large quantities of NADPH-GDH instead of using glutamate synthase pathway. NADP glutamate dehydrogenase 1 Homo sapiens