نتایج جستجو برای: glutamate dehydrogenase gdh

تعداد نتایج: 110978  

2016
Slawomir Michalak Joanna Rybacka-Mossakowska Wojciech Ambrosius Joanna Gazdulska Iwona Gołda-Gocka Wojciech Kozubski Rodryg Ramlau

Objective. To evaluate the involvement of glutamate metabolism in peripheral blood mononuclear cells (PBMC) in the development of neurological complications in lung cancer and during chemotherapy. Methods. The prospective study included 221 lung cancer patients treated with chemotherapeutics. Neurological status and cognitive functions were evaluated at baseline and after 6-month follow-up. Glu...

Journal: :Plant physiology 1991
S K Bhadula P D Shargool

The subcellular distribution of l-glutamate dehydrogenase (GDH, EC 1.4.1.3.) was studied in SB3 soybean (Glycine max) cells using subcellular fractionation techniques. Compounds that inhibit protein synthesis either on 80s or 70s ribosomes were also used to give a preliminary idea of which subcellular fraction is involved in GDH synthesis. It was found that whereas cycloheximide and puromycin c...

Journal: :international journal of advanced biological and biomedical research 2014
shuvasish roy choudhury rita mahanta

ammonia is the chief excretory product in fishes. however, non-availability of enough of water in the habitat, may lead to the formation of urea, in fishes. in the present study, the possible role of urea formation to avoid the toxicity of ammonia under water-restricted condition was tested in channa gachua. circulatory urea and ammonia were estimated in the blood of the fishes and glutamate de...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2007
Dalai Yan

The central nitrogen metabolic circuit in enteric bacteria consists of three enzymes: glutamine synthetase, glutamate synthase (GOGAT), and glutamate dehydrogenase (GDH). With the carbon skeleton provided by 2-oxoglutarate, ammonia/ammonium (NH(4)(+)) is assimilated into two central nitrogen intermediates, glutamate and glutamine. Although both serve as nitrogen donors for all biosynthetic need...

Journal: :Plant physiology 2007
Damianos S Skopelitis Nikolaos V Paranychianakis Antonios Kouvarakis Apostolis Spyros Euripides G Stephanou Kalliopi A Roubelakis-Angelakis

Following the discovery of glutamine synthetase/glutamate (Glu) synthase, the physiological roles of Glu dehydrogenase (GDH) in nitrogen metabolism in plants remain obscure and is the subject of considerable controversy. Recently, transgenics were used to overexpress the gene encoding for the beta-subunit polypeptide of GDH, resulting in the GDH-isoenzyme 1 deaminating in vivo Glu. In this work...

Journal: :The Journal of biological chemistry 2006
Changhong Li Aron Allen Jae Kwagh Nicolai M Doliba Wei Qin Habiba Najafi Heather W Collins Franz M Matschinsky Charles A Stanley Thomas J Smith

Insulin secretion by pancreatic beta-cells is stimulated by glucose, amino acids, and other metabolic fuels. Glutamate dehydrogenase (GDH) has been shown to play a regulatory role in this process. The importance of GDH was underscored by features of hyperinsulinemia/hyperammonemia syndrome, where a dominant mutation causes the loss of inhibition by GTP and ATP. Here we report the effects of gre...

Journal: :Blood 1989
D L Vander Jagt L A Hunsaker M Kibirige N M Campos

Two enzymes from Plasmodium falciparum that catalyze the formation of NADPH have been partially purified and characterized. Glutamate dehydrogenase (GDH), molecular mass 230 Kd, pH optimum 7.0, is capable of producing NADPH under optimum conditions at about 10% of the capacity of the host erythrocyte. This capacity increases slightly during the developmental cycle of the parasite. NADP-specific...

2005
S. W. Leung

This study systematically investigated how anionic surfactants of various hydrophilicities affected the activities of three metabolically important enzymes –– glutamate dehydrogenase (GDH), lactate dehydrogenase (LDH), and malate dehydrogenase (MDH) –– of different molecular masses at a pH range important to body functions (6.5-7.4). We also investigated the time course of the surfactant concen...

Journal: :The Journal of biological chemistry 1999
S W Cho H Y Yoon

The ADP binding site within two types of bovine brain glutamate dehydrogenase isoproteins (GDH I and GDH II) was identified using photoaffinity labeling with [alpha-32P]8-azidoadenosine 5'-diphosphate (8N3ADP). 8N3ADP, without photolysis, mimicked the activatory properties of ADP on GDH I and GDH II activities, although maximal activity with 8N3ADP was about 75% of maximal ADP-stimulated activi...

Journal: :Plant physiology 1986
D E Prunkard N F Bascomb R W Robinson R R Schmidt

Chlorella sorokiniana cells, cultured for 12 hours in 30 millimolar ammonium medium, contained an ammonium inducible nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase (NADP-GDH) isoenzyme with subunits having a molecular weight of 53,000. In vitro translation of total cellular poly(A)(+) RNA, isolated from fully induced cells, resulted in synthesis of an NADP-GDH anti...

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