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1Author    Wemer Jahn, Heinz Faulstich, Axel Deboben, Theodor WielandRequires cookie*
 Title    Formation of Actin Clusters in Rat Liver Parenchymal Cells on Phalloidin Poisoning as Visualized by a Fluorescent Phallotoxin  
 Abstract    By staining of cryo-sections o f rat liver with a fluorescent phallotoxin, the distribution of filamentous actin in liver cells could be demonstrated by fluorescence microscopy. While in untreated livers filamentous actin forms an almost continous layer at the cell periphery, the poisoning by phalloidin leads to the formation of actin clusters, preferentially located near the cell membrane. 
  Reference    Z. Naturforsch. 35c, 467 (1980); received December 28 1979/February 22 1980 
  Published    1980 
  Keywords    Fluorescent Phallotoxin, Actin, Rat Liver 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0467.pdf 
 Identifier    ZNC-1980-35c-0467 
 Volume    35 
2Author    Giinther Harisch, Jürgen ScholeRequires cookie*
 Title    Der Glutathionstatus der Rattenleber in Abhängigkeit vom Lebensalter und von akuter Belastung The Status of Glutathione of the Rat Liver and its Dependence on the Age and Acute Stress  
 Abstract    The status of glutathione in the liver of male rats as a function of their age and acute stress was investigated. Total glutathione (TG), which is measured after the reduction of liver homo-genate with NaBH4 , reduced glutathione (GSH) and disulfide glutathione (GSSG) increase with advancing age of the test animals (weights from 15 g to 350 g). The mixed glutathione disulfides [XSSG = T G — (GSH + 2 G SS G)] of all ages amount to 2.0 fimol/g liver. Subsequent to the application of a stress with Vaccineurin I I I i.p. (weigth of 120 g), the TG values remain the same over a period of 24 hours; GSH decreases 30 min after the stress has been applied, whereas GSSG and XSSG increase. 60 min after the application of Vacci-neurin, all values are within the controlled limits. 24 hours after the stress has been applied, GSH has increased and XSSG has decreased to 0.76 fxmol/g fresh weight, whereas GSSG remains within the controlled limits. The causes of these changes in the status of glutathione are discussed. 
  Reference    (Z. Naturforsch. 29c, 261 [1974]; eingegangen am 2. Januar 1974) 
  Published    1974 
  Keywords    Glutathione Status, Age Dependence, Stress, Rat Liver 
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 TEI-XML for    default:Reihe_C/29/ZNC-1974-29c-0261.pdf 
 Identifier    ZNC-1974-29c-0261 
 Volume    29 
3Author    RitaM. Fink, ErichF. ElstnerRequires cookie*
 Title    Comparison of Different Methods for the Determination of Phenylalanine Hydroxylase Activity in Rat Liver and Euglena gracilis  
 Abstract    Three different methods for the determination of phenylalanine hydroxylase activity have been compared: a) Differential photometric assay of the increase in tyrosine concentration in the presence of phenylalanine; b) Product separation by thin layer chromatography and scintillation counting of the [14C]tyrosine formed; c) HPLC separation and spectrofluorometric quantification of derivatized amino acids. A comparison of the activities of phenylalanine hydroxylase in rat liver and Euglena gracilis clearly showed that only rat liver contains this enzymic activity as shown by methods b) and c) although pseudo-activity of Euglena gracilis preparations was found during the spectrophoto-metric test a). The HPLC method proved to be the fastest, most reliable and convenient method for direct tyrosine determination and thus for measuring phenylalanine hydroxylase activity. 
  Reference    Z. Naturforsch. 39c, 728—733 (1984); received January 27/April 14 1984 
  Published    1984 
  Keywords    Phenylalanine Hydroxylase, Rat Liver, Euglena gracilis, Tyrosine Determination 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0728.pdf 
 Identifier    ZNC-1984-39c-0728 
 Volume    39 
4Author    Meinrad Boll3, LutzW D Webera, Juliana Planac, Andreas Stampfl3, H.M Gcoa ReductaseRequires cookie*
 Title    In Vivo and in Vitro Studies on the Regulatory Link between 3-Hydroxy-3- methylglutaryl Coenzyme A Reductase and Cholesterol 7«-Hydroxylase in Rat Liver  
 Abstract    The activities of 3-hydroxy-3-methylglutaryl CoA reductase (HM GCoA reductase; E C 1.1.1.34), rate-limiting enzyme of cholesterol biosynthesis, and cholesterol 7a-hydroxylase (E C 1.14.13.17), key enzyme of the neutral bile acid synthesis pathway, were measured in the microsomal fraction of rat liver and in rat liver cells to investigate the coordinate regula­ tion of the two pathways. Both enzyme activities exhibited the same diurnal rhythm and responded in a coordinate fashion to fasting or bile acid-feeding (decrease) and to cholestyramine-feeding (increase). Cholesterol-feeding decreased the activity of HMGCoA reductase, increased that of choles­ terol 7a-hydroxylase, and concomitantly increased free cholesterol in microsomes. In an ex vivo setting using primary hepatocytes from animals fed a high cholesterol diet the activity of HM GCoA reductase was initially low and that of cholesterol 7a-hydroxylase was elevated. Release of cholesterol into the medium with ongoing incubation caused H M GCoA reductase activity to increase, and that of cholesterol 7a-hydroxylase to decline. Incubation of hepatocytes with a cholesterol-containing lipoprotein fraction stimulated the activity of cholesterol 7a-hydroxylase, but left HMGCoA reductase activity unaffected. The results confirm the idea of a joint regulation of the two key enzymes of cholesterol metabolism in response to the levels of substrate and metabolites, and support the notion that with respect to bile acid and cholesterol levels, respectively, regulation of HM GCoA reductase activity may be secondary to that of cholesterol 7a-hydroxylase. The in vitro studies supply evidence that the effects of cholesterol and bile acid excess or deficiency are direct and do not involve accessory changes of hormone levels or mediators. 
  Reference    Z. Naturforsch. 54c, 371 (1999); received January 18/March 3 1999 
  Published    1999 
  Keywords    Cholesterol 7a-Hydroxylase, Enzyme Regulation, Cholesterol, Rat Liver 
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 TEI-XML for    default:Reihe_C/54/ZNC-1999-54c-0371.pdf 
 Identifier    ZNC-1999-54c-0371 
 Volume    54 
5Author    RitaM. Fink, ErichF. ElstnerRequires cookie*
 Title    Studies on the Possible Mechanism of Inactivation of Phenylalanine Hydroxylase by Destructive Oxygen Species  
 Abstract    The enzymic hydroxylation of phenylalanine by phenylalanine hydroxylase (E.C. 1.14.16.1.) in vitro is dependent on the presence of hydrogen peroxide removing processes. The loss of phenylalanine hydroxylase activity can be prevented to the same extent by catalase as well as the presence of optimized amounts of both peroxidase and superoxide dismutase. Peroxidase alone exhibited only two third of the maximal protective effect of catalase whereas superoxide dismutase alone was not able to exert any protective influence on phenylalanine hydroxylase. These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H 20 2 and the tetrahydropterin cofactor. 
  Reference    Z. Naturforsch. 39c, 734—737 (1984); received April 24 1984 
  Published    1984 
  Keywords    Phenylalanine Hydroxylase, Rat Liver, Inactivation Mechanism, Destructive Oxygen Species 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0734.pdf 
 Identifier    ZNC-1984-39c-0734 
 Volume    39 
6Author    H.Wolfgang Heger, HorstW. PeterRequires cookie*
 Title    Effects of Phospholipids in the Action of Acetyl-CoA Carboxylase from Rat Liver  
 Abstract    Acetyl-CoA carboxylase (E.C. 6.4.1.2) was isolated from rat liver. The purified enzyme con­ tains phospholipids with a rather large amount of phosphatidylinositol (26%). Incubation of the purified acetyl-CoA carboxylase with phospholipase A2 (E.C. 3.1.1.4) or with phospholipase D (E.C. 3.1.1.4) diminishes the phospholipid content by 70%, this treatment leading to a complete inactivation of the enzyme. After removal of the phospholipases, the lipid-depleted enzyme can be reactivated to a certain degree by incubation with a phospholipid extract from rat liver, with phosphatidylinositol alone, or with serum albumin. 
  Reference    (Z. Naturforsch. 32c, 97 [1977]; received October 12 1976) 
  Published    1977 
  Keywords    Phospholipids, Acetyl-CoA Carboxylase, Rat Liver, Fatty Acid Synthesis, Phospholipases 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0097.pdf 
 Identifier    ZNC-1977-32c-0097 
 Volume    32 
7Author    H. SchimassekRequires cookie*
 Title    Glycogen Synthesis in Rat Liver from a Pool of Free Glucose  
 Abstract    Glycogen synthesis in isolated perfused livers or livers o f anesthetized rats (in situ), was studied using radioactively labelled fructose, lactate, and inositol as substrates. The specific radioactivity o f glucose and glycogen was measured at various times and compared with that o f some intermediates. The results suggest that liver glycogen is formed from the pool o f free glucose which in turn is fed by the so-called "direct and indirect pathway" o f glycogen synthesis. This points to an important role o f glucose-6-phosphatase, an enzyme complex subject to regulation by gluco­ corticoids, well known promoters o f hepatic glycogen synthesis. 
  Reference    Z. Naturforsch. 48c, 85—9 (1993); received September 14 1992 
  Published    1993 
  Keywords    Rat Liver, Glycogen Synthesis, Fructose, G lucocorticoids, Glucose-6-phosphatase 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0085.pdf 
 Identifier    ZNC-1993-48c-0085 
 Volume    48 
8Author    Meinrad Boll3, LutzW D W Eberb, A.Ndreas Stampflb, Burkhard Messner3Requires cookie*
 Title    Lipogenic Enzymes of Rat Liver and Adipose Tissue. Dietary Variations and Effect of Polychlorinated Biphenyls  
 Abstract    The lipogenic enzymes fatty acid synthase (FAS; EC 2.3.1.85), citrate cleavage enzyme (CCE; EC 4.1.3.8), malic enzyme (ME; EC 1.1.1.40), glucose-6-phosphate dehydrogenase (G6PDH; EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (PGDH; EC 1.1.1.44) were investigated in liver and in brown adipose tissue (BAT) of Wistar rats under various dietary conditions and in the presence of 15 to 250 ppm (approximately 0.045-0.75 [.imol/kg chow) polychlorinated biphenyls (PCBs). In response to refeeding starved animals, enzyme activities in both tissues increased to above normal levels and thereafter exhibited pronounced oscillations of their activities. The extent of increase depended on the carbohydrate and fat content of the diet. The lipogenic enzymes could be grouped in two categories according to their sensitivity to dietary carbo­ hydrate: FAS and CCE responded faster to smaller changes in dietary composition, while ME, G6PDH and PGDH required larger changes and more time to respond. Diet-induced alterations of enzyme activities were of the same order of magnitude in liver and BAT. They were age-dependent, being more pronounced in young animals. Independent of the type of dietary manipulations, activities changed in a coordinate fashion, i.e., the changes of the activities of all 5 enzymes occurred at similar ratios to each other with an identical time course. Feeding PCB-containing diets resulted in a considerable increase of the activities of the lipogenic enzymes in liver, which was significantly greater with ME, G 6PD H and PGDH. The effect was dose-dependent but transient. In liver the response to PCB feeding was iden­ tical in male and female animals, whereas in BAT lipogenic activities increased in females, but decreased in males. Refeeding starved animals with a PCB-containing diet led to an additional stimulation of the normal refeeding-induced increase of the enzyme activities in liver and BAT. This PCB-induced increase was 2-fold for FAS and CCE, but up to 15-fold for the other enzymes. All PCB-induced effects were significantly less pronounced in old than in young animals. In primary hepatocytes activities increased in hormone-free medium in the presence of PCBs. While activity was induced in insuline-and triiodothyronine-containing medium, this increase was significantly greater with PCBs present. 
  Reference    Z. Naturforsch. 49c, 665—678 (1994); received May 5/July 14 1994 
  Published    1994 
  Keywords    Lipogenic Enzymes, Rat Liver, Brown Adipose Tissue, Hepatocytes, Polychlorinated Biphenyls 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0665.pdf 
 Identifier    ZNC-1994-49c-0665 
 Volume    49 
9Author    Meinrad Bolla, LutzW D W Eberbc, A.Ndreas StampflbRequires cookie*
 Title    The Effect of y-Hexachlorocyclohexane (Lindane) on the Activities of Liver Lipogenic Enzymes and on Serum Lipids in Rats  
 Abstract    The effect of dietary y-hexachlorocyclohexane (lindane) (5 0 -3 5 0 ppm, 0 .1 7 -1 .1 9 |imol/kg chow) on the activity of enzymes of lipogenesis, viz., fatty acid synthase (FAS; EC 2.3.1.85), citrate cleavage enzyme (CCE; EC 4.1.3.8), malic enzym e (ME; EC 1.1.1.40), glucose-6-phos-phate dehydrogenase (G 6 PDH; EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (PGDH; EC 1.1.1.44), and on serum lipid levels, was investigated in livers of 35-day-old male Wistar rats. Lindane (150 ppm) caused a substantial decline of enzym e activities within the first 24 h of treatment. The decrease was transient, however, and enzyme activities subsequently recov­ ered despite continuation of lindane feeding. The recovery of enzyme activities was compara­ tively fast in the case of ME, G 6 PDH and PG D H , but very slow with FAS and CCE. A ctivities of lipogenic enzymes decrease when animals are starved, and increase much beyond prestarvation levels upon subsequent refeeding. Lindane in the refeeding diet blunted this overshoot of FAS and CCE activities in a dose-dependent manner. In contrast, activities of ME, G 6 PD H and P G D H responded to low dietary lindane concentrations with a substantial stimulation of the increase o f activity, whereas at high lindane concentrations the overshoot was inhibited. According to their responses to lindane exposure, liver lipogenic enzymes could be grouped into 2 categories with FAS and CCE representing one and ME, G 6 PDH and PG D H representing the other group. Polychlorinated biphenyls (PCBs) in the diet caused basically opposite changes of the activities of the lipogenic enzymes. Co-administration o f lindane and PCBs resulted in an apparent cancellation of effects, suggesting that lindane and PCBs affect fatty acid synthesis at opposite points. Levels of the serum triglycerides were increased significantly as a result of lindane feeding, while serum cholesterol and phospholipid levels were only slightly elevated. The increase of serum triglyceride levels that is routinely observed after refeeding o f starved animals was stimulated even more by low concentrations o f lindane in the refeeding diet, but inhibited by high concentrations. 
  Reference    Z. Naturforsch. 50c, 135 (1995); received August 9/September 16 1994 
  Published    1995 
  Keywords    Lipogenic Enzymes, Rat Liver, y-H exachlorocyclohexane (Lindane), Enzyme Regulation, Serum Lipids 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0135.pdf 
 Identifier    ZNC-1995-50c-0135 
 Volume    50