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Liver mitochondrial

Dubey RK, Beg MU, Singh J. 1984. Effects of endosulfan and its metabolites on rat liver mitochondrial respiration and enzyme activities in vitro. Biochem Pharmacol 33 3405-3410. [Pg.283]

Hayakawa, M., Ogawa, T., Sugiyama, S., Tanaka, M. and Ozawa, T. (1991). Massive conversion of guanine to 8-hydroxyguanosine in mouse liver mitochondrial DNA by administration of azidothymidine. Biochem. Biophys. Res. Commun. 176, 87-93. [Pg.212]

Zhou J, Weiner H. Basis for half-of-the-sites reactivity and the dominance of the K487 oriental subunit over the E487 subunit in heterotetrameric human liver mitochondrial aldehyde dehydrogenase. Biochemistry 2000 39 12019-12024... [Pg.437]

LOX catalyzed the oxidation of arachidonoylphosphatidylcholine at both carbon-12 and carbon-15. Later on, it has been found [21] that reticulocyte lipoxygenase oxidized rat liver mitochondrial membranes, beef heart submitochondrial particles, rat liver endoplasmic membranes, and erythrocyte plasma membranes without preliminary release of unsaturated acids by phospholipases. [Pg.808]

Figure 1. Influence of time on metabolism of I4C-DEHP by trout liver mitochondrial and microsomal fractions. Incubation contained 0.010 /imol of 14C-DEPH in a total volume of 2 mL. Mitochondria equivalent to 0.254 g of liver or microsomes equivalent to 0.361 g of liver were used in each incubation. Open bars represent monoester, striped bars Polar Metabolite I and solid bars Polar Metabolite 2. Each column represents an individual incubation (14). Figure 1. Influence of time on metabolism of I4C-DEHP by trout liver mitochondrial and microsomal fractions. Incubation contained 0.010 /imol of 14C-DEPH in a total volume of 2 mL. Mitochondria equivalent to 0.254 g of liver or microsomes equivalent to 0.361 g of liver were used in each incubation. Open bars represent monoester, striped bars Polar Metabolite I and solid bars Polar Metabolite 2. Each column represents an individual incubation (14).
Axen E, Postlind H, Sjoberg H, Wikvall K. 1994. Liver mitochondrial cytochrome P450 CYP27 and recombinant-expressed human CYP27 catalyze 1 alpha-hydroxylation... [Pg.81]

When fatty add p-oxidation predominates in the liver, mitochondrial pyruvate is most likely to be... [Pg.204]

In 1998, Pedersen, Amzel, and colleagues solved the X-ray structure of rat liver mitochondrial Fj-ATPase to 2.8 A resolution and obtained a more symmetrical structure of the a and (3 subunits [27]. In this structure, catalytic as well as non-catalytic sites are occupied with bound nucleotide and the three a subunits and the three (3 subunits are in very similar but distinct closed conformations, with no indication of an open conformation as found in the Walker structure. The rat liver crystals were grown in the presence of substantially higher concentrations of nucleotides, and the crystallization medium contained only ATP (and not AMP-PNP),butno Mg +. [Pg.71]

M.C. Walker, D.E. Edmondson, Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B, Biochemistry 33 (1994) 7088-7098. [Pg.690]

Sus scrofa (acidic adenylate kinase from pig heart resembles liver mitochondrial enzyme [14]) [3, 13-16]... [Pg.493]

In tissues such as of the liver, mitochondrial activities such as fatty acid metabolism are compromised, and the liver eventually fails with potentially fatal consequences. [Pg.313]

An alkaline pyrophosphatase from rat liver cytoplasm has been partially purified and characterized (24) the corresponding enzyme from mice is inhibited by Mg J+-ADP and free PPj, and free Mg2+ has been implicated as an allosteric activator (23). Partial heat inactivation results in loss of the apparent allosteric effects. Rat liver mitochondrial pyrophosphatase, which is inhibited by adenine nucleotides (36), appears to be bound to the inside of the inner mitochondrial membrane (37). This enzyme, after solubilization, has been separated into two fractions which have somewhat different specificity (24, 38). A pyrophosphatase strongly simulated by sulfhydryl reagents (39) has been partially purified from brain tissue (40). The mono-magnesium PPj complex appears to be the true substrate for this enzyme (41). Pynes and Younathan have purified a pyrophosphatase 1800-fold from human erythrocytes (43). The properties of this enzyme are strikingly similar to those of the yeast enzyme the major difference appears to be the more rigid substrate specificity of the erythrocyte enzyme in the presence of Znz. ... [Pg.540]

In 1960, Rafter (32) first described an activity in mouse liver mitochondrial preparations which was capable of catalyzing the hydrolysis of PPi and the transfer of a phosphoryl group from PPi to glucose to produce glucose-6-P [reaction (3a)]. This same activity was also observed... [Pg.546]

Lieser, M.J., Park, J., Natori, S., Jones, B. A., Bronk, S. F., and Gores, G. J., 1998, Cholestasis confers resistance to the rat liver mitochondrial permeability transition, Gastroenterology 115, pp. 693-701 Litsky, M.L. and Pfeiffer, D. R., 1997, Regulation of the mitochondrial Ca2+ uniporter by external adenine nucleotides the uniporter behaves like a gated channel which is regulated by nucleotides and divalent cations, Biochemistry 36, pp. 7071—7080... [Pg.502]

Wodtke, E. (1978). Lipid adaptation in liver mitochondrial membranes of carp acclimated to different environmental temperatures. Phospholipid composition, fatty acid pattern and cholesterol content. Biochimica etBiophysicaActa 529,280-291. [Pg.322]

Gpxl-deficient mice Increase in ROS level and in lipid peroxidation level in liver decrease in liver mitochondrial respiratory control ratio and power output index Growth retardation E3... [Pg.106]

Fountoulakis M, Berndt P, Langen H, Suter L. The rat liver mitochondrial proteins. Electrophoresis 2002 23 311-328. [Pg.432]

Hutson, SM Berkich, D Williams, G.D., La Noue, K.F., Briggs, R.W. (1989). 31P NMR visibility and characterization of rat liver mitochondrial matrix adenine nucleotides. Biochemistry 28, 4325-4332. [Pg.266]

Yu and coworkers measured the substrate specificity of rat liver mitochondrial thioesterase, which hydrolyzes acyl-CoA to CoA and free fatty acid (see Chapter 21). This enzyme was approximately twice as active with C14-CoA thioesters as with Ci8-CoA thioesters. [Pg.196]

Mitochondrial oxidative stress and mitochondrial GSH defense affects transcription factor activation. Oxidant stress in mitochondria not only can promote the loss of mitochondrial GSH and mitochondrial functions, but also can promote extramito-chondrial activation of NF-kB and therefore may affect nuclear gene expression. Mitochondria are targets of cytokines leading to the overproduction of reactive oxygen species induced by ceramide, a lipid intermediate of cytokine action and closely associated with apoptosis. Chronic ethanol intake depletes liver mitochondrial glutathione due to an ethanol-induced defect in the transport of GSH from cytosol into the mitochondrial matirix. This sensitizes liver cells to the prooxidant effects of cytokines and prooxidants generated by the oxidative metabolism of ethanol. [Pg.350]

Quandt L and Huth W (1984) Modulation of rat-liver mitochondrial acetyl-CoA acetyl-transferase activity by a reversible chemical modification with coenzyme A. Biochim-ica et BiophysicaActa 784,168-76. [Pg.447]

Jeevaratnam, K., Vidya, S., Vaidyanathan, C.S. (1992h). In vitro and in vivo effect of methyl isocyanate on rat liver mitochondrial respiration. Toxicol. Appl. Pharmacol. 117 172-9. [Pg.309]

Studies performed by the authors of this review [142,144], suggest that the discrepancies are due to functional microcompartmentation between the aspartate aminotransferase and the aspartate transporter. The apparent for aspartate efflux can be dramatically decreased by generation of intramitochondrial aspartate by the aminotransferase reaction. Detailed isotopic studies using labelled matrix aspartate in liver mitochondrial [142] and labelled intramitochondrial glutamate in kidney mitochondria [144] confirmed the initial suggestion. [Pg.237]

DEF has been reported to cause extensive alterations in morphological features of erythrocyte and nuclear membranes and affected the permeability properties of rat liver mitochondrial membrane. A reduction in the activity of cytochrome-c-oxidase and NAD. H-oxidase has also been observed. Content of both DNA and RNA decreased in tissues studied within 1 month of DEF intoxication and was usually restored within 3 months. Histological study showed development of necrodystrophy in liver tissue and of fibroplastic glomerulonephritis in kidney. The deteriorating effect of DEF on cellular genome functions... [Pg.731]


See other pages where Liver mitochondrial is mentioned: [Pg.208]    [Pg.195]    [Pg.593]    [Pg.86]    [Pg.124]    [Pg.124]    [Pg.527]    [Pg.530]    [Pg.546]    [Pg.147]    [Pg.493]    [Pg.128]    [Pg.254]    [Pg.110]    [Pg.115]    [Pg.171]    [Pg.6]    [Pg.56]    [Pg.561]    [Pg.3]    [Pg.314]    [Pg.12]    [Pg.135]    [Pg.223]   
See also in sourсe #XX -- [ Pg.172 ]




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