نتایج جستجو برای: succinate dehydrogenase

تعداد نتایج: 75966  

Journal: :The Journal of biological chemistry 1968
G Palmer D J Horgan H Tisdale T P Singer H Beinert

On the addition of NADH to submitochondrial particles in which NADH oxidase is blocked by rotenone, piericidin A, or Amytal, the g = 1.94 signal of NADH dehydrogenase appears in essentially the same manner as in untreated preparations. However, the appearance of the NADHinduced iron signal of succinate dehydrogenase and of cytochromes b and cl is inhibited by these agents. It is concluded that ...

Journal: :The Journal of biological chemistry 1976
D L Cinti S R Keyes M A Lemelin H Denk J B Schenkman

The oxidation of formaldehyde by rat liver mitochondria in the presence of 50 mM phosphate was enhanced 2-fold by exogenous NAD+. Absolute requirement of NAD+ for formaldehyde oxidation was demonstrated by depleting the mitochondria of their NAD+ content (4.6 nmol/mg of protein), followed by reincorporation of the NAD+ into the depleted mitochondria. Aldehyde (formaldehyde) dehydrogenase activi...

2001
Peter Owen

Using EPR spectroscopy to monitor the integrity of the enzyme, conditions have been established which allow specific immunoprecipitation of the succinate dehydrogenase complex of Escherichia coli. The enzyme complex precipitated from Lubrol PX-solubilized membranes by monospecific antiserum in the presence of a cocktail of protease inhibitors contains four polypeptides of apparent Mrs 71,000,26...

2013
Sewha Kim Do Hee Kim Woo-Hee Jung Ja Seung Koo

The aim of this study was to investigate succinate dehydrogenase (SDH) expression in breast cancer according to breast cancer molecular subtype using immunohistochemistry and to assess the clinical implications of SDH expression. Immunohistochemical staining for ER, PR, HER-2, Ki-67, HIF-1α, SDHA, and SDHB was performed on tissue microarrays of 721 breast cancers. According to the immunohistoch...

Journal: :Journal of bacteriology 1973
M E Spencer J R Guest

Escherichia coli produces two enzymes which interconvert succinate and fumarate: succinate dehydrogenase, which is adapted to an oxidative role in the tricarboxylic acid cycle, and fumarate reductase, which catalyzes the reductive reaction more effectively and allows fumarate to function as an electron acceptor in anaerobic growth. A glycerol plus fumarate medium was devised for the selection o...

Journal: :Physiological research 2012
H Rauchová M Vokurková Z Drahota

Digitonin solubilizes mitochondrial membrane, breaks the integrity of the respiratory chain and releases two mobile redox-active components: coenzyme Q (CoQ) and cytochrome c (cyt c). In the present study we report the inhibition of glycerol-3-phosphate- and succinate-dependent oxygen consumption rates by digitonin treatment. Our results show that the inhibition of oxygen consumption rates is r...

Journal: :The Journal of biological chemistry 1980
B A Ackrell M B Ball E B Kearney

A preparation has been made from Complex I1 of beef heart mitochondria which contains in purified form two peptides, designated CItw3 and Ctt-4, with molecular weights of 13,500 and 7,000, respectively. Recombination of soluble succinate dehydrogenase with the peptides elicits ubiquinone reductase activity and, with Complex 111, antimycin-sensitive cytochrome c reductase activity, while the “lo...

Journal: :Toxicology in vitro : an international journal published in association with BIBRA 2001
G Repetto A del Peso P Sanz M Repetto

Lithium and nickel present low toxicity, but are able to cause alterations in different tissues. The toxic effects of lithium and nickel at different cellular levels were assessed using two inorganic chemical species: lithium chloride and nickel(II) chloride. Mouse neuroblastoma cell cultures (Neuro-2a) were exposed to both compounds for 24 h. The cytotoxic effects evaluated were cell prolifera...

Journal: :Current opinion in plant biology 2013
Shaobai Huang A Harvey Millar

Succinate dehydrogenase (SDH) oxidises succinate to fumarate as a component of the tricarboxylic acid cycle and ubiquinone to ubiquinol in the mitochondrial electron transport chain. Studies of SDH mutants have revealed far-reaching effects of altering succinate oxidation in plant cells. The plant SDH complex composition, structure and assembly are all beginning to be understood but the implica...

2014
Ildiko Pecsi Kiel Hards Nandula Ekanayaka Michael Berney Travis Hartman William R. Jacobs Gregory M. Cook

UNLABELLED Succinate:quinone oxidoreductase (Sdh) is a membrane-bound complex that couples the oxidation of succinate to fumarate in the cytoplasm to the reduction of quinone to quinol in the membrane. Mycobacterial species harbor genes for two putative sdh operons, but the individual roles of these two operons are unknown. In this communication, we show that Mycobacterium smegmatis mc(2)155 ex...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید