نتایج جستجو برای: ژن nadh dehydrogenase subunit 2 nd2
تعداد نتایج: 2651438 فیلتر نتایج به سال:
in the present study, mitochondrial dna polymerase chain reaction-restriction fragment length polymorphism (pcr-rflp) assay was used to assess the population structure and genetic relationships among six persian sturgeon, acipenser persicus populations from south caspian sea along the iranian coast. the complete nucleotide dehydrogenase subunit 5 (nadh 5) region of mtdna amplified by pcr was di...
Complex I is the first and largest enzyme in the respiratory chain located in the inner mitochondrial membrane and in the membrane of many bacteria [1]. In the process of oxidizing NADH, Complex I translocates 4 protons across the membrane. This is followed by additional proton translocation by complexes III and IV. The resulting membrane potential powers ATP production by the F-ATPase. The min...
Seven of the approximately 40 subunits of the mammalian respiratory NADH dehydrogenase (Complex I) are encoded in mitochondrial DNA (mtDNA). Their function is almost completely unknown. In this work, a novel selection scheme has led to the isolation of a mouse A9 cell derivative defective in NADH dehydrogenase activity. This cell line carries a near-homoplasmic frameshift mutation in the mtDNA ...
Electron-transferring flavoproteins (ETF) are heterodimeric enzymes that contain FAD and which transfer reducing equivalents between other flavoenzymes. In mitochondria they accept reducing equivalents from reduced forms of fatty acyl CoA dehydrogenases, sarcosine dehydrogenase, and dimethylglycine dehydrogenase and transfer them to a third flavoenzyme that reduces Coenzyme Q. ETF has similar f...
Bacterial 3alpha-hydroxysteroid dehydrogenase, which belongs to a short-chain dehydrogenase/reductase family and forms a dimer composed of two 26-kDa subunits, catalyzes the oxidoreduction of hydroxysteroids in a coenzyme-dependent manner. This enzyme also catalyzes the oxidoreduction of nonsteroid compounds that play an important role in xenobiotic metabolism of bacteria. We performed an x-ray...
NADH dehydrogenase of Escherichia coli, a component of the electron transport chain, oxidizes NADH to NAD. Previously, it was demonstrated that when E. coli K12 cells were lysed by the lysozyme lysis method, NADH dehydrogenase activity was inhibited; however, when cells were lysed by French press, NADH dehydrogenase activity was observed. In this study, components commonly used in lysozyme lysi...
Ocean Acidification (OA) is known to affect various aspects of physiological performances of diatoms, but little is known about the underlining molecular mechanisms involved. Here, we show that in the model diatom Phaeodactylum tricornutum, the expression of key genes associated with photosynthetic light harvesting as well as those encoding Rubisco, carbonic anhydrase, NADH dehydrogenase and ni...
Little is known of the biology and diversity of the environmental model genus Daphnia beyond the Nearctic and western Palearctic. Here, we describe Daphnia sinevi sp. nov., a species superficially similar to Daphnia curvirostris Eylmann, 1878, from the Far East of Russia. We estimated its phylogenetic position in the subgenus Daphnia s. str. with a rapidly evolving mitochondrial protein coding ...
A small number of cetaceans have adapted to an entirely freshwater environment, having colonized rivers in Asia and South America from an ancestral origin in the marine environment. This includes the 'river dolphins', early divergence from the odontocete lineage, and two species of true dolphins (Family Delphinidae). Successful adaptation to the freshwater environment may have required increase...
In the present study, mitochondrial DNA polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) assay was used to assess the population structure and genetic relationships among six Persian sturgeon, Acipenser persicus populations from south Caspian Sea along the Iranian coast. The complete nucleotide dehydrogenase subunit 5 (NADH 5) region of mtDNA amplified by PCR was di...
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