نتایج جستجو برای: glutamate dehydrogenase

تعداد نتایج: 110753  

Journal: :Journal of Biological Chemistry 1970

Journal: :jundishapur journal of microbiology 0
elham sadat roointan parasitology department, faculty of medicine, ahvaz jundishapur university of medical sciences, ahvaz, ir iran abdollah rafiei parasitology department, faculty of medicine, and infectious and tropical diseases research center, ahvaz jundishapur university of medical sciences, ahvaz, ir iran; parasitology department, faculty of medicine, and infectious and tropical diseases research center, ahvaz jundishapur university of medical sciences, ahvaz, ir iran.tel:+ 98-6112230540, fax:+ 98-6112231325 ali reza samarbaf-zadeh virology department, faculty of medicine, ahvaz jundishapur university of medical sciences, ahvaz, ir iran ali akbar shayesteh department of internal medicine, imam khomeini hospital, faculty of medicine, ahvaz jundishapur university of medical sciences, ahvaz, ir iran ahmad shamsizadeh pediatreic department and infectious and tropical diseases research center, ahvaz jundishapur university of medical sciences, ahvaz, ir iran mahdi pourmahdi borujeni department of food hygiene, faculty of veterinary medicine, shahid chamran university of ahvaz, ahvaz, ir iran

background giardia lamblia is an enteric protozoan parasite, which infects human and a wide range of vertebrate hosts. objectives the aim of this study was to investigate genotypes of g. lamblia from children fecal samples in ahvaz, south west of iran by pcr-rflp method. materials and methods fecal samples were collected from 58 children who were positive for g. lamblia. dna extractions were pe...

Journal: :Journal of bacteriology 2008
Fabian M Commichau Katrin Gunka Jens J Landmann Jörg Stülke

Glutamate is a central metabolite in all organisms since it provides the link between carbon and nitrogen metabolism. In Bacillus subtilis, glutamate is synthesized exclusively by the glutamate synthase, and it can be degraded by the glutamate dehydrogenase. In B. subtilis, the major glutamate dehydrogenase RocG is expressed only in the presence of arginine, and the bacteria are unable to utili...

Journal: :Anesthesia and analgesia 2007
Gong-Jhe Wu Zhi-Hong Wen Wu-Fu Chen Yi-Chen Chang Chen-Hwan Cherng Chih-Shung Wong

BACKGROUND Excitatory amino acids play an important role in morphine tolerance. Recently, we demonstrated that a single morphine challenge induces an increase in spinal cerebrospinal fluid excitatory amino acid concentrations in morphine-tolerant rats, and that dexamethasone inhibits the development of morphine tolerance. We further examined the effect of intrathecal dexamethasone infusion on t...

Journal: :European Journal of Biochemistry 2005

Journal: :The Journal of biological chemistry 1965
G M Tomkins K L Yielding J F Curran M R Summers M W Bitensky

Glutamate dehydrogenase (L-glutamate-NAD(P) oxidoreductase EC 1.4.1.3) from bovine liver catalyzes the reversible oxidative deamination of various monocarboxylic amino acids, as well as of n-glutamate (1, 2). Several years ago, we reported that estrogenic steroids both inhibited the oxidation of L-glutamate (3) and stimulated the oxidation of L-alanine (4). Conversely, adenosine diphosphate was...

Journal: :The Journal of biological chemistry 1974
L A Fahien S E Smith

Glutamate dehydrogenase decreases the distribution COefficient of glutamate oxalacetate transaminase in Sephadex G-ZOO. This is consistent with previous results which suggested that a complex is formed between these two enzymes. These gel filtration as well as kinetic experiments suggest that transaminase can react with monomeric but not polymer forms of glutamate dehydrogenase. When the levels...

Journal: :Journal of bacteriology 1981
J F Kane J Wakim R S Fischer

The activity of the nicotinamide adenine dinucleotide-dependent glutamate dehydrogenase in Bacillus subtilis was influenced by the carbon source, but not the nitrogen source, in the growth medium. The highest specific activity for this enzyme was found when B. subtilis was grown in a minimal or rich medium that contained glutamate as the carbon source. It is proposed that glutamate dehydrogenas...

Journal: :Journal of bacteriology 1990
S M Miller B Magasanik

We cloned GDH2, the gene that encodes the NAD-linked glutamate dehydrogenase in the yeast Saccharomyces cerevisiae, by purifying the enzyme, making polyclonal antibodies to it, and using the antibodies to screen a lambda gt11 yeast genomic library. A yeast strain with a deletion-disruption allele of GDH2 which replaced the wild-type gene grew very poorly with glutamate as a nitrogen source, but...

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