Effect of dietary protein on the DPNH cytochrome c reductase activity of rat liver

1962 ◽  
Vol 96 (3) ◽  
pp. 672-674 ◽  
Author(s):  
Fiorenzo Stirpe ◽  
Klaus Schwarz
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Dietary Protein ◽  
Reductase Activity ◽  
Cytochrome C Reductase

scholarly journals Immunochemical characterization of NADPH-cytochrome P-450 reductase from Jerusalem artichoke and other higher plants

1989 ◽  
Vol 259 (3) ◽  
pp. 847-853 ◽  
Author(s):  
I Benveniste ◽  
A Lesot ◽  
M P Hasenfratz ◽  
F Durst
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Higher Plants ◽  
Polyclonal Antibodies ◽  
Reductase Activity ◽  
Jerusalem Artichoke ◽  
Cross Reactivity ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Cytochrome P 450

Polyclonal antibodies were prepared against NADPH-cytochrome P-450 reductase purified from Jerusalem artichoke. These antibodies inhibited efficiently the NADPH-cytochrome c reductase activity of the purified enzyme, as well as of Jerusalem artichoke microsomes. Likewise, microsomal NADPH-dependent cytochrome P-450 mono-oxygenases (cinnamate and laurate hydroxylases) were efficiently inhibited. The antibodies were only slightly inhibitory toward microsomal NADH-cytochrome c reductase activity, but lowered NADH-dependent cytochrome P-450 mono-oxygenase activities. The Jerusalem artichoke NADPH-cytochrome P-450 reductase is characterized by its high Mr (82,000) as compared with the enzyme from animals (76,000-78,000). Western blot analysis revealed cross-reactivity of the Jerusalem artichoke reductase antibodies with microsomes from plants belonging to different families (monocotyledons and dicotyledons). All of the proteins recognized by the antibodies had an Mr of approx. 82,000. No cross-reaction was observed with microsomes from rat liver or Locusta migratoria midgut. The cross-reactivity generally paralleled well the inhibition of reductase activity: the enzyme from most higher plants tested was inhibited by the antibodies; whereas Gingko biloba, Euglena gracilis, yeast, rat liver and insect midgut activities were insensitive to the antibodies. These results point to structural differences, particularly at the active site, between the reductases from higher plants and the enzymes from phylogenetically distant plants and from animals.

scholarly journals Asymmetric distribution of cytochrome P-450 and NADPH–cytochrome P-450 (cytochrome c) reductase in vesicles from smooth endoplasmic reticulum of rat liver

1980 ◽  
Vol 190 (3) ◽  
pp. 737-746 ◽  
Author(s):  
Michael B. Cooper ◽  
John A. Craft ◽  
Margaret R. Estall ◽  
Brian R. Rabin
Keyword(s):  
Endoplasmic Reticulum ◽  
Cytochrome C ◽  
Rat Liver ◽  
Smooth Endoplasmic Reticulum ◽  
Reductase Activity ◽  
Asymmetric Distribution ◽  
Trypsin Treatment ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Cytochrome P 450

1. The topography of cytochrome P-450 in vesicles from smooth endoplasmic reticulum of rat liver has been examined. Approx. 50% of the cytochrome is directly accessible to the action of trypsin in intact vesicles whereas the remainder is inaccessible and partitioned between luminal-facing or phospholipid-embedded loci. Analysis by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis reveals three major species of the cytochrome. Of these, the variant with a mol.wt. of 52000 is induced by phenobarbitone and this species is susceptible to trypsin. 2. After trypsin treatment of smooth membrane, some NADPH–cytochrome P-450 (cytochrome c) reductase activity remains and this remaining activity is enhanced by treatment with 0.05% deoxycholate, which renders the membranes permeable to macromolecules. In non-trypsin-treated control membranes the reductase activity is increased to a similar extent. These observations suggest an asymmetric distribution of NADPH–cytochrome P-450 (cytochrome c) reductase in the membrane. 3. As compared with dithionite, NADPH reduces only 44% of the cytochrome P-450 present in intact membranes. After tryptic digestion, none of the remaining cytochrome P-450 is reducible by NADPH. 4. In the presence of both a superoxide-generating system (xanthine plus xanthine oxidase) and NADPH, all the cytochrome P-450 in intact membrane (as judged by dithionite reducibility) is reduced. The cytochrome P-450 remaining after trypsin treatment of smooth vesicles cannot be reduced by this method. 5. The superoxide-dependent reduction of cytochrome P-450 is prevented by treatment of the membranes with mersalyl, which inhibits NADPH–cytochrome P-450 (cytochrome c) reductase. Thus the effect of superoxide may involve NADPH–cytochrome P-450 reductase and cytosolically orientated membrane factor(s).

Brain Regional Analysis of NADH-Cytochrome C Reductase Activity in Alzheimerʼs Disease

1990 ◽  
Vol 49 (3) ◽  
pp. 206-214 ◽  
Author(s):  
GEORGE S. ZUBENKO ◽  
JOHN MOOSSY ◽  
DIANA CLAASSEN ◽  
A. Julio Martinez ◽  
GUTTI R. RAO
Keyword(s):  
Cytochrome C ◽  
Reductase Activity ◽  
Regional Analysis ◽  
Cytochrome C Reductase ◽  
Nadh Cytochrome

STUDIES ON THE CYTOCHROME OXIDASE AND OXIDATION PATHWAY IN UREDOSPORES OF WHEAT STEM RUST

1961 ◽  
Vol 39 (5) ◽  
pp. 1131-1148 ◽  
Author(s):  
G. A. White ◽  
G. A. Ledingham
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Reductase Activity ◽  
Oxygen Affinity ◽  
Antimycin A ◽  
Respiratory Enzymes ◽  
Wheat Stem Rust ◽  
Malic Dehydrogenase ◽  
Cytochrome C Reductase

Electron transport to oxygen in a particulate fraction from uredospores of Puccinia graminis var. tritici occurs through a series of carriers similar to those of other fungi and higher plants.Experiments with various enzyme inhibitors and measurements of the oxygen affinity of respiration have shown that cytochrome oxidase mediates the final step in the sequence of electron transfer. The enzyme was localized in a fraction sedimenting at 20,000 g and was typically inhibited by cyanide, azide, and CO-dark, the latter inhibition being light-reversible. Other enzymes present were succinic-cytochrome c reductase, DPNH- and TPNH-cytochrome c reductase, dye reductase, malic dehydrogenase, isocitric dehydrogenase, and glycerol-1-phosphate dehydrogenase. Particulates failed to oxidize DPNH unless an electron acceptor was added. An increase in the activity of several of the respiratory enzymes was noted upon spore germination.Succinic-cytochrome c reductase was only partially sensitive to Antimycin A, HOQNO, and the naphthoquinone, SN 5949. These compounds markedly inhibited a labile portion of the DPNH-cytochrome c reductase activity but had little effect on the stable activity remaining in aged particles. Menadione, but not vitamin K1, stimulated electron transfer. Antimycin A and SN 5949 virtually blocked spore respiration suggesting a "Slater-type" factor in the intact pathway of oxidation.

scholarly journals Re-examination of the subcellular localization of thyroxine 5′-deiodination in rat liver

1979 ◽  
Vol 180 (2) ◽  
pp. 273-279 ◽  
Author(s):  
D Auf Dem Brinke ◽  
R D Hesch ◽  
J Köhrle
Keyword(s):  
Endoplasmic Reticulum ◽  
Cytochrome C ◽  
Subcellular Localization ◽  
Rat Liver ◽  
Marker Enzyme ◽  
Cytochrome C Reductase ◽  
Substrate Saturation ◽  
Single Enzyme ◽  
Optimal Ph ◽  
Nadph Cytochrome C Reductase

We describe the existence of at least two thyroxine 5′-deiodinases in rat liver. They co-fractionate with NADPH-cytochrome c reductase, the marker enzyme for membranes of the endoplasmic reticulum. Subcellular-localization studies of the most active microsomal thyroxine 5′-deiodinase were performed under substrate saturation and at optimal pH 6.8. This enzyme was a Km(app.) of about 3 microM-thyroxine and a Vmax. of about 8 ng of tri-iodothyronine/min per mg of protein. Our study confirms in part the earlier reports of microsomal localization of thyroxine 5′-deiodination. However, this process is not mediated by only a single enzyme.

Temperature Influence on Basal Activity and Induction of Mixed Function Oxygenase Activity in Fundulus heteroclitus

1979 ◽  
Vol 36 (11) ◽  
pp. 1400-1405 ◽  
Author(s):  
John J. Stegeman
Keyword(s):  
Cytochrome C ◽  
Fundulus Heteroclitus ◽  
Reductase Activity ◽  
Control Fish ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Pyrene Hydroxylase ◽  
Mixed Function Oxygenase ◽  
Cytochrome P 450 ◽  
Nadph Cytochrome C Reductase

Treatment of Fundulus heteroclitus acclimated to 6.5 °C with benzo(a)pyrene did not elicit any change in the levels of hepatic microsomal NADH- or NADPH-cytochrome c reductase activity, nor in the levels of cytochrome P-450 or its catalytic activities. However, the same treatment offish at 16 5 °C resulted in a marked induction of benzo(a)pyrene hydroxylase and NADPH-cytochrome c reductase. Cytochrome P-450 content was also higher in the warm, treated fish and the Soret maximum of reduced, CO-treated microsomes was shifted to the violet. Levels of aminopyrine demethylase and NADH-cytochrome c reductase activities did not show a significant treatment effect. At neither temperature could treated and control fish be distinguished on the basis of in vitro inhibition of benzo(a)pyrene hydroxylase activity by 7,8-benzoflavone. Levels of NADPH-cytochrome c reductase and benzo(a)pyrene hydroxylase activities were greater in control Fundulus acclimated to 6.5 °C than to 16.5 °C, when normalized to microsomal protein, but not when based on body weight. The results indicate that habitat temperature alone may not affect the capacity for initial hydrocarbon metabolism in fish, but that it can strongly influence the induction of cytochrome P-450. Key words: temperature, cytochrome P-450, hydrocarbon metabolism, mixed-function oxygenase, Fundulus heteroclitus

Assignment of estradiol-17β dehydrogenase and of estrone reductase to cytoplasmic structures of porcine endometrium cells

1989 ◽  
Vol 121 (2) ◽  
pp. 161-167 ◽  
Author(s):  
J. Adamski ◽  
W. D. Sierralta ◽  
P. W. Jungblut
Keyword(s):  
Cytochrome C ◽  
Kinetic Data ◽  
Reductase Activity ◽  
Particulate Fraction ◽  
Marker Enzyme ◽  
Structural Element ◽  
Cytochrome C Reductase ◽  
Percoll Gradients ◽  
Cytoplasmic Structures ◽  
Estradiol 17Β

Abstract. Homogenates of porcine endometrium contain substantial activity for the dehydrogenation of estradiol-17β but little for estrone reduction. Both activities are associated with cytoplasmic structures. The dehydrogenase is characterized by a pH 7.7 optimum, Km 2.2 × 10−7 mol/l for estradiol and Km 4.4 × 10−5 mol/l for the cosubstrate NAD+. The corresponding figures for the reductase are pH 6.6, Km 1.1 × 10−6 mol/1 for estrone and Km 2.1 × 10−5 mol/l for the cosubstrate NADPH. The (mitochondrial/lysosomal) 17 000 × g particulate fraction contains a 52-fold higher dehydrogenase than reductase activity. The (microsomal) 200000 × g particulate fraction is only 16-fold richer in dehydrogenase. Isopycnic centrifugations of the two fractions in Percoll gradients reveal that estrone reductase and the coequilibrating marker enzyme cytochrome c reductase occur in constant proportions, whereas the dehydrogenase/cytochrome c reductase ratios are different. Both, the kinetic data and the structural assignments speak in favour of individual enzymes catalyzing the dehydrogenation of estradiol and the reduction of estrone. All gradient fractions exhibiting dehydrogenase activity feature small, electrondense vesicles of 0.15–0.20 μm in diameter as a common structural element which might harbour the dehydrogenase.

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