Log in

Relevant bibliographies by topics / Rat liver mitochondria

Contents

Journal articles
Dissertations / Theses
Books
Book chapters
Conference papers
Reports

Academic literature on the topic 'Rat liver mitochondria'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Rat liver mitochondria.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Rat liver mitochondria"

1

Shibata, Tatsuya, Toshinari Takahashi, Eio Yamada, Akiko Kimura, Hiroshi Nishikawa, Hiroyoshi Hayakawa, Nobuhiko Nomura, and Junichi Mitsuyama. "T-2307 Causes Collapse of Mitochondrial Membrane Potential in Yeast." Antimicrobial Agents and Chemotherapy 56, no. 11 (September 4, 2012): 5892–97. http://dx.doi.org/10.1128/aac.05954-11.

Full text

Abstract:

ABSTRACTT-2307, an arylamidine compound, has been previously reported to have broad-spectrumin vitroandin vivoantifungal activities against clinically significant pathogens, includingCandidaspecies,Cryptococcus neoformans, andAspergillusspecies, and is now undergoing clinical trials. Here we investigated the mechanism of action of T-2307 using yeast cells and mitochondria isolated from yeast and rat liver. Nonfermentative growth ofCandida albicansandSaccharomyces cerevisiaein glycerol medium, in which yeasts relied on mitochondrial respiratory function, was inhibited at 0.001 to 0.002 μg/ml (0.002 to 0.004 μM) of T-2307. However, fermentative growth in dextrose medium was not inhibited by T-2307. Microscopic examination using Mitotracker fluorescent dye, a cell-permeant mitochondrion-specific probe, demonstrated that T-2307 impaired the mitochondrial function ofC. albicansandS. cerevisiaeat concentrations near the MIC in glycerol medium. T-2307 collapsed the mitochondrial membrane potential in mitochondria isolated fromS. cerevisiaeat 20 μM. On the other hand, in isolated rat liver mitochondria, T-2307 did not have any effect on the mitochondrial membrane potential at 10 mM. Moreover, T-2307 had little inhibitory and stimulatory effect on mitochondrial respiration in rat liver mitochondria. In conclusion, T-2307 selectively disrupted yeast mitochondrial function, and it was also demonstrated that the fungal mitochondrion is an attractive antifungal target.

APA, Harvard, Vancouver, ISO, and other styles

2

Stuhne-Sekalec, Lidija, and Nikola Z. Stanacev. "Mechanism and localization of cardiolipin biosynthesis revisited: evidence for the identical mechanism and different localization in mitochondrial and submitochrondrial membranes isolated from guinea pig and rat liver." Biochemistry and Cell Biology 68, no. 6 (June 1, 1990): 922–35. http://dx.doi.org/10.1139/o90-137.

Full text

Abstract:

The mechanism of cardiolipin (diphosphatidylglycerol) biosynthesis was examined in mitochondria and outer and inner mitochondrial membranes prepared from guinea pig and rat livers to determine whether this formation from phosphatidylglycerol was absolutely dependent on cytidinediphosphodiglyceride, as previously reported for intact mitochondria. Experimental results confirmed that the biosynthesis of cardiolipin, from the membrane-bound radioactive phosphatidylglycerol in intact mitochondria isolated from guinea pig and rat liver, was absolutely dependent on CDP-diglycerides and required the addition of divalent cations. Furthermore, the same mechanism for the biosynthesis of cardiolipin was operational in the outer and inner mitochondrial membranes. This biosynthesis was associated with both the outer and inner mitochondrial membranes prepared from guinea pig liver, but only with the inner mitochondrial membranes prepared from rat liver. The release of radioactive glycerol was also measured, but the amount obtained did not satisfy the stoichiometric requirement for CDP-diglyceride-independent biosynthesis of cardiolipin from 2 mol of phosphatidylglycerol with the liberation of 1 mol of glycerol. Therefore, it was concluded that this mechanism is not involved in the biosynthesis of cardiolipin in mitochondrial and submitochondrial membranes prepared from guinea pig and rat liver.Key words: mitochondria, outer mitochondrial membranes, inner mitochondrial membranes, cardiolipin, biosynthesis.

APA, Harvard, Vancouver, ISO, and other styles

3

Azain, M. J., and J. A. Ontko. "An explanation for decreased ketogenesis in the liver of the obese Zucker rat." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 257, no. 4 (October 1, 1989): R822—R828. http://dx.doi.org/10.1152/ajpregu.1989.257.4.r822.

Full text

Abstract:

These studies were undertaken to further characterize and explain the differences in hepatic fatty acid metabolism between lean and obese Zucker rats. It was shown that the rate of palmitate or octanoate oxidation and the inhibition of palmitate oxidation by malonyl CoA in mitochondria isolated from lean and obese Zucker rats were similar. Cytochrome oxidase activity was similar in lean and obese rat livers. It was found that the addition of cytosol from the obese rat liver inhibited palmitate oxidation by 20-30% in mitochondria isolated from lean or obese rat livers and thus reproduced the conditions observed in the intact cell. Increased concentrations of metabolites such as malonyl CoA and glycerophosphate in the liver of the obese rat are likely contributors to this inhibitory effect. These results are extrapolated to the intact cell and suggest that decreased hepatic fatty acid oxidation in the obese rat can be accounted for by cytosolic influences on the mitochondria. The decreased rate of fatty acid oxidation observed in the intact hepatocyte or perfused liver cannot be explained by a defect in the capacity of mitochondria to oxidize substrate or by a decrease in mitochondrial number in the obese rat liver.

APA, Harvard, Vancouver, ISO, and other styles

4

Goudarzi, M., H. Kalantari, and M. Rezaei. "Glyoxal toxicity in isolated rat liver mitochondria." Human & Experimental Toxicology 37, no. 5 (June 22, 2017): 532–39. http://dx.doi.org/10.1177/0960327117715900.

Full text

Abstract:

Glyoxal is a physiological metabolite formed by lipid peroxidation, ascorbate autoxidation, oxidative degradation of glucose, and degradation of glycated proteins. Glyoxal has been linked to oxidative stress and can cause a number of cellular damages, including covalent modification of amino and thiol groups of proteins to form advanced glycation end products. However, the mechanism of glyoxal toxicity has not been fully understood. In this study, we have focused on glyoxal toxicity in isolated rat liver mitochondria. Isolated mitochondria (0.5 mg protein per milliliter) were prepared from the Wistar rat liver using differential centrifugation and incubated with various concentrations of glyoxal (1, 2.5, 5, 7.5, and 10 mM) for 30 min. The activity of mitochondrial complex II was determined by measurement of MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) conversion. The mitochondrial membrane potential (MMP), lipid peroxidation (MDA), reactive oxygen species (ROS) formation, glutathione (GSH) content, and protein carbonylation were also assessed. After an incubation of isolated liver mitochondria with glyoxal, disrupted electron transport chain, increased mitochondrial ROS formation, lipid peroxidation, mitochondrial membrane damage, GSH oxidation, and protein carbonylation ensued as compared to the control group ( p < 0.05). Glyoxal toxicity in isolated rat liver mitochondria was dose-dependent. In conclusion, glyoxal impaired the electron transport chain, which is the cause of increased ROS and MDA production, depletion of GSH, and disruption of MMP. Mitotoxicity of glyoxal might be related to the pathomechanisms involved in diabetes and its complications.

APA, Harvard, Vancouver, ISO, and other styles

5

Heine, U. I., J. K. Burmester, K. C. Flanders, D. Danielpour, E. F. Munoz, A. B. Roberts, and M. B. Sporn. "Localization of transforming growth factor-beta 1 in mitochondria of murine heart and liver." Cell Regulation 2, no. 6 (June 1991): 467–77. http://dx.doi.org/10.1091/mbc.2.6.467.

Full text

Abstract:

Using both electron microscopic immunohistochemistry and cell fractionation techniques, we show that transforming growth factor-beta 1 (TGF-beta 1) is found in mitochondria of rat and mouse cardiac myocytes and rat hepatocytes. Four different polyclonal antibodies, raised against various epitopes encompassing the mature portion of the TGF-beta 1 molecule as well as the pro-region of its precursor, were used for the electron microscopy studies. The localization of TGF-beta 1 in mitochondria was confirmed by detection of the native peptide in mitochondria isolated from rat heart and liver; the majority of native TGF-beta 1 found in liver homogenates was recovered in highly pure mitochondrial fractions. The functional role of TGF-beta in the mitochondrion is unknown at present.

APA, Harvard, Vancouver, ISO, and other styles

6

Freeman, M., and E. H. Mangiapane. "Translocation to rat liver mitochondria of phosphatidate phosphohydrolase." Biochemical Journal 263, no. 2 (October 15, 1989): 589–95. http://dx.doi.org/10.1042/bj2630589.

Full text

Abstract:

When a particle-free supernatant fraction from rat liver was incubated at 37 degrees C with mitochondria and oleate, some of the enzyme phosphatidate phosphohydrolase (PAP), initially present in the particle-free supernatant, was recovered, after the incubation, bound to mitochondria. This translocation of PAP from cytosol to mitochondria was stimulated by oleate or palmitate in a similar fashion to the stimulation of translocation of PAP to endoplasmic reticulum [Martin-Sanz, Hopewell & Brindley (1984) FEBS Lett. 175, 284-288]. Translocation of PAP from particle-free supernatant to a partially purified mitochondrial-outer-membrane preparation was also stimulated by oleate. More PAP was bound to a mitochondrial-outer-membrane fraction washed in 0.5 M-NaCl before resuspension in sucrose than to a sucrose-washed mitochondrial-outer-membrane preparation. In contrast, washing of microsomal membranes in 0.5 M-NaCl did not enhance the binding of PAP to these membranes. PAP also binds to phosphatidate-loaded mitochondria or microsomes (microsomal fractions). In the experimental system employed, more PAP bound to mitochondria loaded with phosphatidate than to microsomes loaded with phosphatidate. The results are discussed in relation to the role of mitochondrial phosphatidate in liver lipid metabolism.

APA, Harvard, Vancouver, ISO, and other styles

7

Quant, P. A., P. K. Tubbs, and M. D. Brand. "Treatment of rats with glucagon or mannoheptulose increases mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase activity and decreases succinyl-CoA content in liver." Biochemical Journal 262, no. 1 (August 15, 1989): 159–64. http://dx.doi.org/10.1042/bj2620159.

Full text

Abstract:

1. The activity of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase (EC 4.1.3.5) in extracts of rapidly frozen rat livers was doubled in animals treated in various ways to increase ketogenic flux. 2. Some 90% of the activity measured was mitochondrial, and changes in mitochondrial activity dominated changes in total enzyme activity. 3. The elevated HMG-CoA synthase activities persisted throughout the isolation of liver mitochondria. 4. Intramitochondrial succinyl-CoA content was lower in whole liver homogenates and in mitochondria isolated from animals treated with glucagon or mannoheptulose. 5. HMG-CoA synthase activity in mitochondria from both ox and rat liver was negatively correlated with intramitochondrial succinyl-CoA levels when these were manipulated artificially. Under these conditions, the differences between mitochondria from control and hormone-treated rats were abolished. 6. These findings show that glucagon can decrease intramitochondrial succinyl-CoA concentration, and that this in turn can regulate mitochondrial HMG-CoA synthase. They support the hypothesis that the formation of ketone bodies from acetyl-CoA may be regulated by the extent of succinylation of mitochondrial HMG-CoA synthase.

APA, Harvard, Vancouver, ISO, and other styles

8

Beggs, M., and P. J. Randle. "Activity of branched-chain 2-oxo acid dehydrogenase complex in rat liver mitochondria and in rat liver." Biochemical Journal 256, no. 3 (December 15, 1988): 929–34. http://dx.doi.org/10.1042/bj2560929.

Full text

Abstract:

Four mitochondrial marker enzymes were used to show that: (1) high-protein (24%) diet increased the rat liver concentration and content of total branched-chain 2-oxo acid dehydrogenase complex (BCDC) by 31% by increasing mitochondrial specific activity of BCDC; (2) starvation increased the liver concentration of BCDC by 25% by decreasing liver weight; the liver content of mitochondria and the mitochondrial specific activity of BCDC were unchanged; (3) protein-free diet decreased rat liver BCDC concentration and content by 20%, by decreasing the liver concentration and content of mitochondria. Protein-free diet increased liver mitochondrial specific activities of L-glutamate, 2-oxoglutarate and NAD-isocitrate dehydrogenases. The validity of a mitochondrial method for the determination of the liver concentration of BCDC and the percentage in the active form in vivo is confirmed, and improvements are described. The experimental basis of criticisms of its use in this regard by Zhang, Paxton, Goodwin, Shimomura & Harris [(1987) Biochem. J. 246, 625-631] was not confirmed. The finding by Harris, Powell, Paxton, Gillim & Nagae [(1985) Arch. Biochem. Biophys. 243, 542-555], that starvation has no effect on the percentage of BCDC in the active form in rat liver, is confirmed.

APA, Harvard, Vancouver, ISO, and other styles

9

Espinal, J., P. A. Patston, H. R. Fatania, K. S. Lau, and P. J. Randle. "Purification and properties of a protein activator of phosphorylated branched-chain 2-oxo acid dehydrogenase complex." Biochemical Journal 225, no. 2 (January 15, 1985): 509–16. http://dx.doi.org/10.1042/bj2250509.

Full text

Abstract:

The protein activator of phosphorylated branched-chain 2-oxo acid dehydrogenase complex was purified greater than 1000-fold from extracts of rat liver mitochondria; the specific activity was greater than 1000 units/mg of protein (1 unit gives half-maximum re-activation of 10 munits of phosphorylated complex). Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis gave two bands (Mr 47700 and 35300) indistinguishable from the alpha- and beta-subunits of the branched-chain dehydrogenase component of the complex. On gel filtration (Sephacryl S-300), apparent Mr was 190000. This and other evidence suggests that activator protein is free branched-chain dehydrogenase; this conclusion is provisional until identical amino acid composition of the subunits has been demonstrated. Activator protein (i.e. free branched-chain dehydrogenase) was inhibited (up to 30%) by NaF, whereas branched-chain complex was not inhibited. There was no convincing evidence for interconvertible active and inactive forms of activator protein in rat liver mitochondria. Activator protein was detected in mitochondria from liver (ox, rabbit and rat) and kidney (ox and rat), but not in rat heart or skeletal-muscle mitochondria. In rat liver mitochondrial extracts, branched-chain complex sedimented with the mitochondrial membranes, whereas activator protein remained in the supernatant. Activator protein re-activated phosphorylated (inactive) particulate complex from rat liver mitochondria, but it did not activate dephosphorylated complex. Liver and kidney, but not muscle, mitochondria apparently contain surplus free branched-chain dehydrogenase, which is bound by the complex with lower affinity than is the branched-chain dehydrogenase intrinsic to the complex. It is suggested that this functions as a buffering mechanism to maintain branched-chain complex activity in liver and kidney mitochondria.

APA, Harvard, Vancouver, ISO, and other styles

10

Carlenor, Elisabeth, Vigg Joste, B. Dean Nelson, and Jan Rydström. "Cell-free translation of mitochondrial nicotinamide nucleotide transhydrogenase." Bioscience Reports 5, no. 6 (June 1, 1985): 483–90. http://dx.doi.org/10.1007/bf01116947.

Full text

Abstract:

Mammalian nicotinamide nucleotide transhydrogenase is translated as a 5000 daltons larger molecular weight precursor in a cell-free system programmed with rat liver polysomes. The mature rat liver enzyme had the same molecular weight as the purified beef heart enzyme, 115 000 daltons. The precursor was not processed in vitro by liver mitochondria or by a rat liver mitochondrial matrix fraction, nor did it appear to bind to mitochondria. In contrast, pre-FeS protein of the cytochrome bc1 complex was processed in the same samples by both mitochondria and matrix, suggesting an important difference in the processing mechanisms or in the efficiency of processing of the two precursors.

APA, Harvard, Vancouver, ISO, and other styles

More sources

Dissertations / Theses on the topic "Rat liver mitochondria"

1

Harris, Jonathan Malcolm. "The glutathione S-transferases of rat liver mitochondria." Thesis, University College London (University of London), 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325084.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Denyer, G. "Regulation of hepatic pyruvate dehydrogenase complex by reversible phosphorylation." Thesis, University of Oxford, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.233529.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Halle-Smith, Simon C. "A study of the inner membrane anion channel of rat liver mitochondria." Thesis, University of East Anglia, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.277348.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Marshall, Myles C. B. "Molecular properties of carnitine palmitoyltransferases I and II from rat liver mitochondria." Thesis, University of Edinburgh, 1993. http://hdl.handle.net/1842/12571.

Full text

Abstract:

CPT I was localised in the outer mitochondrial membrane and then partially purified. The protein was digested with restriction endonucleases and the fragments N-terminally sequenced and used to generate oligonucleotides for cDNA library screening and polymerase chain reaction (PCR). The partially purified protein was also used to generate polyclonal antibodies, which were used to screen λgt11 cDNA libraries. A positive clone was isolated from the λgt11 cDNA library using affinity purified serum. When sequenced, the clone was identified as long chain fatty acid CoA synthase. CPT II was purified from rat liver mitochondrial inner membranes and n-terminally sequenced. The purified protein was used to generate polyclonal antibodies. Oligonucleotides were generated to the cDNA encoding CPT II reported by Woeltje et al (1990b) and used to PCR up a 300 bp fragment, which when cloned and sequenced was identified as the C-terminus of CPT II. This fragment was then used unsuccessfully to screen λgt10, λgt11 and λgt11-stretch cDNA libraries, in order to find a full length clone. Using the information generated by this thesis along with other recent publications a possible topology of CPT I in the rat liver mitochondrial outer membrane was elucidated.

APA, Harvard, Vancouver, ISO, and other styles

5

Sutherland, Steven Thomas. "Studies on the metabolism of oxalate, glyoxylate, glycolate and glycine by peroxisomes and mitochondria from rat liver /." The Ohio State University, 1991. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487693923196163.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Sibille, Brigitte. "Modulation de l'effet découplant du 2,4-dinitrophenol en fonction des substrats : étude sur hépatocytes isolés de rat." Université Joseph Fourier (Grenoble ; 1971-2015), 1998. http://www.theses.fr/1998GRE10199.

Full text

Abstract:

Le couplage mitochondrial entre oxydation des substrats et phosphorylation est variable et la capacite de dissocier ces deux reactions joue un role primordial dans les phenomenes de regulation du metabolisme cellulaire (production de chaleur, regulation de la production d'especes radicalaires et de la masse corporelle). Nous avons etudie dans ce travail les consequences d'un decouplage de l'oxydation phosphorylante par le 2,4-dinitrophenol sur le metabolisme intermediaire et sur l'etat energetique d'hepatocytes isoles ainsi que la modulation de ce decouplage en fonction des substrats utilises. En presence d'hydrates de carbone (dihydroxyacetone), le decouplage mitochondrial par le 2,4-dinitrophenol, du fait de l'augmentation de la permeabilite de la membrane mitochondrial interne aux protons, conduit a une diminution du potentiel de membrane mitochondrial. Ce qui induit une inhibition de la synthese mitochondriale d'atp qui conduit a l'arret de la neoglucogenese. Ensuite, du fait de l'inhibition des fonctions de la navette malate-aspartate (electrogenique), les potentiels redox cytosolique et mitochondrial se rapprochent de l'equilibre thermodynamique. Il en resulte une oxydation mitochondriale qui induit une inhibition de la respiration. En presence d'octanoate ou de proline, substrats fournissant des equivalents reduits dans la matrice, une augmentation du potentiel de membrane mitochondrial d'hepatocytes decouples est mesuree. Celle ci entraine une augmentation de la synthese mitochondriale d'atp, de la neoglucogenese, de l'activite de la navette malate-aspartate et enfin de la respiration cellulaire. De plus, nous avons observe que le decouplage a des consequences differentes suivant les pompes de la chaine respiratoire etudiees. Les effets sont importants sur le potentiel de membrane et sur la synthese d'atp maintenus par le complexe iii alors que le decouplage est sans effet sur le complexe iv. En conclusion, le decouplage mitochondrial regulateur du metabolisme cellulaire peut etre module par les substrats utilises donc par le regime choisi (hydrates de carbones vs acides gras) et ses consequences sont differents suivant les voies metaboliques etudiees (respiration vs neoglucogenese).

APA, Harvard, Vancouver, ISO, and other styles

7

Benba, Jamila. "Contribution à l'étude du système de transport des dicarboxylates des mitochondries; purification, caractérisation." Rouen, 1993. http://www.theses.fr/1993ROUES053.

Full text

Abstract:

Le travail presenté dans ce mémoire a été entrepris dans le but de purifier et de caractériser le transporteur des dicarboxylates des mitochondries, qui catalyse l'échange un contre un des dicarboxylates entre eux (malate, malonate, succinate) ou contre le phosphate. Cette étude a été effectuée simultanément sur les mitochondries de foie de rat et sur les mitochondries d'une souche de levure: Saccharomyces cerevisiae. Les mitochondries de levure ont été solubilisées par le Triton X-100 et l'extrait a été chromatographié sur hydroxyapatite. Le filtrat, traité par électrophorèse en milieu dénaturant, a révélé par coloration à l'argent la présence d'environ 5 protéines de Mr compris entre 28000 et 35000. Après reconstitution de l'activité de transport dans des liposomes, un accroissement de 10 fois, de l'activité spécifique d'échange a été observé. Le passage des protéines du filtrat d'hydroxyapatite sur une colonne de malate deshydrogénase mitochondriale (EC 1. 1. 1. 37) immobilisée sur Sépharose, a conduit à la purification complète du transporteur. Cette protéine, purifiée à partir des deux types de mitochondries, possède toutes les propriétés caractéristiques du transporteur in situ et présente, en milieu dénaturant, un poids moléculaire de 28000. L'activité du transporteur purifié à partir des mitochondries de levure, reconstituée dans des liposomes, montre un Km pour le succinate de 2 mM et un Vmax de 1,5 lmol. Min-1. Mg-1 protéines tandis que l'activité spécifique augmente de 300 fois par rapport à l'extrait de départ. L'activité d'échange du transporteur reconstituée des deux types de mitochondries est inhibée par un réactif des groupements SH, le p-chloromercuriphénylsulfonate et par un réactif des acides aminés, le phosphate de pyridoxal, suggérant l'implication d'un ou plusieurs groupements SH et d'un ou plusieurs résidus lysine dans le mécanisme catalytique du transporteur. L'analyse de la composition en acides aminés de la protéine de transport des mitochondries de foie de rat indique qu'il s'agit d'une protéine hydrophobe, légèrement acide, avec la partie N-terminale bloquée

APA, Harvard, Vancouver, ISO, and other styles

8

Masmoudi, Ahmed. "Etude de l'ADP-ribosylation dans les mitochondries." Grenoble 2 : ANRT, 1988. http://catalogue.bnf.fr/ark:/12148/cb37615884v.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Senior, David John Carleton University Dissertation Chemistry. "Isolation, structural and mechanistic studies of rat liver mitochondrial aldehyde dehydrogenase." Ottawa, 1987.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

10

Petit, Patrice-Xavier. "Mitochondries, membranes mitochondriales et interactions sub-cellulaires : aspects métaboliques, sites récepteurs, potentiel de membrane, propriétés de surface et homogénéité des populations." Paris 6, 1988. http://www.theses.fr/1988PA066686.

Full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

Books on the topic "Rat liver mitochondria"

1

Halle-Smith, Simon C. A study of the inner membrane anion channel of rat liver mitochondria. Norwich: University of East Anglia, 1990.

Find full text

APA, Harvard, Vancouver, ISO, and other styles

2

Clarke, Andrew. Temperature and reaction rate. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780199551668.003.0007.

Full text

Abstract:

All other things being equal, physiological reaction rate increases roughly exponentially with temperature. Organisms that have adapted over evolutionary time to live at different temperatures can have enzyme variants that exhibit similar kinetics at the temperatures to which they have adapted to operate. Within species whose distribution covers a range of temperatures, there may be differential expression of enzyme variants with different kinetics across the distribution. Enzymes adapted to different optimum temperatures differ in their amino acid sequence and thermal stability. The Gibbs energy of activation tends to be slightly lower in enzyme variants adapted to lower temperatures, but the big change is a decrease in the enthalpy of activation, with a corresponding change in the entropy of activation, both associated with a more open, flexible structure. Despite evolutionary adjustments to individual enzymes involved in intermediary metabolism (ATP regeneration), many whole-organism processes operate faster in tropical ectotherms compared with temperate or polar ectotherms. Examples include locomotion (muscle power output), ATP regeneration (mitochondrial function), nervous conduction and growth.

APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Rat liver mitochondria"

1

Frei, Balz, and Christoph Richter. "Mono(ADP-Ribosyl)ation in Rat Liver Mitochondria." In ADP-Ribose Transfer Reactions, 433–36. New York, NY: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4615-8507-7_82.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Watkins, Linda, and Roger A. Lewis. "Carrier Mediated Uptake of Deoxyguanosine in Rat Liver Mitochondria." In Purine and Pyrimidine Metabolism in Man V, 85–88. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_14.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Szewczyk, Adam, Stawomir Pikuła, Lech Wojtczak, and Maciej J. Nałęczl. "ATP-Sensitive K+ Channel in Rat Liver Mitochondria: Functional Characteristics." In Molecular Biology of Mitochondrial Transport Systems, 221–28. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78936-6_16.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Macedo, Denise V., Valmir L. Ferraz, Lucia Pereira-da-Silva, and Anibal E. Vercesi. "Ca2+-Dependent NAD(P)+-Induced Alterations in Membrane Permeability of Rat Liver Mitochondria." In Integration of Mitochondrial Function, 535–42. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2551-0_52.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Díaz-Achirica, P., S. Prieto, J. Ubach, D. Andreu, E. Rial, and L. Rivas. "Permeabilization of rat liver mitochondria by cecropin A-melittin hybrid peptides." In Peptides 1994, 777–78. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_358.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Vamecq, Joseph, and Jean-Pierre Draye. "Beta-Oxidation of Omega-Hydroxymonocarboxylic Acids in Rat Liver Peroxisomes and Mitochondria." In Lipid Storage Disorders, 395–403. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1029-7_48.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Cantatore, Palmiro, Flavio Fracasso, Angela Maria Serena Lezza, and Maria Nicola Gadaleta. "Regulation of the Expression of COI and COIII mRNAs in Rat Liver Mitochondria." In Cytochrome Systems, 153–59. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_22.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Tomasi, Aldo, Emanuele Albano, Barbara Botti, Francesco P. Corongiu, M. Assunta Dessì, Anna Iannone, Valeria Franceschi, Vanio Vannini, and Alberto Masini. "Lipid Peroxidation and Bioactivation of Halogenated Hydrocarbons in Rat Liver Mitochondria During Experimental Siderosis." In Chemical Carcinogenesis, 143–51. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4757-9640-7_16.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Augustin, Wolfgang, Ingrid Wiswedel, Heiko Noack, Thomas Reinheckel, and Olaf Reichelt. "Role of endogenous and exogenous antioxidants in the defence against functional damage and lipid peroxidation in rat liver mitochondria." In Detection of Mitochondrial Diseases, 199–205. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-6111-8_31.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Palmi, M., F. Fusi, G. Youmbi, M. Frosini, L. Bianchi, L. Della Corte, G. P. Sgaragli, and K. F. Tipton. "Effects of Taurine and Structurally Related Analogues on Ca2+ Uptake and Respiration Rate in Rat Liver Mitochondria." In Advances in Experimental Medicine and Biology, 117–24. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-0182-8_14.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Rat liver mitochondria"

1

Lee, Hsien-Chang, NaiGuang Wang, and Britton Chance. "Characterization of rat liver mitochondria using time-resolved spectroscopy." In OE/LASE'93: Optics, Electro-Optics, & Laser Applications in Science& Engineering, edited by Britton Chance and Robert R. Alfano. SPIE, 1993. http://dx.doi.org/10.1117/12.154642.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

GOLEVA, T. N., A. G. ROGOV, K. K. EPREMYAN, G. P. SHUMAKOVICH, and R. A. ZVYAGILSKAYA. "EFFECTS OF SKQN ON RAT LIVER MITOCHONDRIA AND YEAST CELLS." In HOMO SAPIENS LIBERATUS. TORUS PRESS, 2020. http://dx.doi.org/10.30826/homosapiens-2020-41.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Ovsyannikova, Tatyana N., Irina A. Zabelina, Alexandr N. Levchenko, Tatyana A. Rybka, Vasiliy A. Svitch, and Vladimir V. Tovstyak. "Effect of low intensity laser irradiation on rat liver mitochondria." In 2008 International Conference on Advanced Optoelectronics and Lasers (CAOL). IEEE, 2008. http://dx.doi.org/10.1109/caol.2008.4671945.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Passarella, S., S. Molinari, E. Casamassima, D. Pastore, E. Quagliariello, I. M. Catalano, and A. Cingolani. "He-Ne laser irradiation influences oxidative phosphorylation in isolated rat liver mitochondria in vitro." In Conference on Lasers and Electro-Optics. Washington, D.C.: OSA, 1985. http://dx.doi.org/10.1364/cleo.1985.wm45.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Kang, Young Bok (Abraham), Joseph Cirillo, Siddhartha Rawat, Michael Bouchard, and Hongseok (Moses) Noh. "Layered Hepatocytes and Endothelial Cells on a Transwell Membrane: Toward Engineering the Liver Sinusoid." In ASME 2012 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/imece2012-89413.

Full text

Abstract:

This paper presents a novel liver model platform that mimics the liver sinusoid, a functional unit of the liver where most liver activities occur. A key component of the current liver model is a layered co-culture of primary rat hepatocytes (PRH) and primary rat liver sinusoidal endothelial cells (LSEC) or a bovine aortic endothelial cells (BAEC) as an alternative. Poly-dimethylsiloxane (PDMS) microchannels were fabricated and attached to transwell membranes that contain submicroscale pores. Cells were cultured either on one side or on both sides of the transwell membrane, and in both cases cells formed confluent layers. A thin matrigel coating or micro porous membrane was applied between the two cell layers in order to mimic the Space of Disse. We used three different methods to check cell viability: recombinant adenovirus expressing green fluorescent protein, mito-tracker red to stain live mitochondria, and an expression plasmid expressing red fluorescent protein (RFP). It was shown that PRH retained normal morphology and remained viable for about 3 days with BAEC in the PDMS microchannel, about 57 days with BAEC on the transwell, and about 39 days with primary LSEC on the transwell. Preliminary observation suggests that there is formation of structures between hepatocytes that appear similar to bile canaliculi when PRH are co-cultured with endothelial cells. The layered co-culture system seems to be a promising method to generate accurate liver models.

APA, Harvard, Vancouver, ISO, and other styles

6

Ovsyannikova, Tatyana, Alina Kovalenko, Irina Zabelina, Natalya Hmil, Tetiana Mishchenko, Aleksandr Gladkih, and Aleksandr Levchenko. "Effect of Low Intensity Laser Irradiation as well as Visible and Infra-Red Polarized Irradiation on Rat Liver Mitochondria." In 2019 IEEE 8th International Conference on Advanced Optoelectronics and Lasers (CAOL). IEEE, 2019. http://dx.doi.org/10.1109/caol46282.2019.9019514.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

IMADA, I., EF SATO, R. KONAKA, M. NISHIKAWA, Y. KIRA, A.-M. PARK, Q. LI, and M. INOUE. "EFFECTS OF CALORIC RESTRICTION AND AGING ON THE GENERATION OF REACTIVE OXYGEN SPECIES IN RAT LIVER MITOCHONDRIA AND PEROXISOMES." In Proceedings of the 13th International Symposium. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812702203_0069.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Lepore, Giovanna, Erica Miranda, César Henrique Yokomizo, Lucca Cassiavilani, Iseli Lourenço Nantes, and Nasser Ali Daghastanli. "Kinetics of Photobleaching of Methylene Blue in a Collagen Matrix in the Absence and Presence of Isolated Rat Liver Mitochondria." In Latin America Optics and Photonics Conference. Washington, D.C.: OSA, 2014. http://dx.doi.org/10.1364/laop.2014.lth4a.27.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Lu, De-Zhao, Ping-Er Wang, Ji Zhu, Tao-Qi Lin, and Xing-De Wo. "Effect of Hydrocortisone on Liver Mitochondria Proteome of Rats." In 2012 International Conference on Biomedical Engineering and Biotechnology (iCBEB). IEEE, 2012. http://dx.doi.org/10.1109/icbeb.2012.168.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Ovsyannikova, Tatyana, Irina Zabelina, and Alexander Levchenko. "Influence of Low Intencity Laser Radiation on Functions of Mitochondria in Rats' Liver." In 2006 International Workshop on Laser and Fiber-Optical Networks Modeling. IEEE, 2006. http://dx.doi.org/10.1109/lfnm.2006.252093.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Rat liver mitochondria"

1

Palmeira, Carlos. Low-dose, Chronic Exposure to Silver Nanoparticles Causes Mild Mitochondrial Alterations in the Liver of Sprague-Dawley Rat. Fort Belvoir, VA: Defense Technical Information Center, May 2014. http://dx.doi.org/10.21236/ada611639.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!