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  • Articles: DFG German National Licenses  (4)
  • rat heart  (2)
  • Acylglycerol lipase  (1)
  • Chemostat  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism 875 (1986), S. 76-86 
    ISSN: 0005-2760
    Keywords: (Rat heart) ; Acylglycerol lipase ; Lipolytic enzyme
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 135 (1983), S. 199-204 
    ISSN: 1432-072X
    Keywords: Rhizobium leguminosarum ; Nitrogenase ; Acetylene reduction ; Growth yields ; Chemostat ; Fedbatch
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rhizobium leguminosarum is capable of nitrogen fixation in free living cultures. Nitrogenase activity can be induced when the ammonia supply of a nitrogen-limited culture, in which the oxygen concentration is regulated at 1 μm, is switched off. Assuming a nitrogen content of the cell of 12% the theoretical washout curve of such a culture can be calculated. The measured optical densities are higher than the calculated ones. In one case, 8 days after the shift, the medium supply was switched off and batch growth with molecular nitrogen occurred. Acetylene reduction started immediately in samples taken 2 days after the shift. Addition of ammonium chloride to the test vials inhibited acetylene reduction. The highest specific activities were found 5–8 days after the shift (100 nmol ethylene formed per milligram dry weight per hour). From this activity a μmax of 0.007–0.009 (generation time 76–98 h) on molecular nitrogen can be calculated. After the shift Y mannitol decreased from 33 to 23 in the first 48 h. Three days after the shift Y mannitol had a value of 15. During batch growth Y mannitol had a value of 8. In a carbon-limited fed-batch culture R. leguminosarum shows three distinct growth phases with different values of Y mannitol. This is an indication for a stringent response in the third growth phase, and probably nitrogen fixation occurs under stringent response situations.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Basic research in cardiology 79 (1984), S. 268-273 
    ISSN: 1435-1803
    Keywords: rat heart ; lipolysis ; lysosomes ; interstitium ; glycerol release ; myocardium ; lipoprotein lipase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Mobilization of triacylglycerol stored in heart cells is accomplished by the combined action of lysosomal (acid) lipase and microsomal monoacylglycerol lipase or carboxylesterase. Non(heparin)-releasable neutral or alkaline lipase is similar to non(readily)-releasable lipoprotein lipase (LPL). The enzyme is mainly localized extracellularly. Non(readily)-releasable LPL probably represents LPL in caveola or vacuolae of vascular endothelium and/or LPL on myocardial interstitium. It contributes to the uptake of lipoprotein constituents in heart cells. Glycerol, an endproduct of lipolysis, is not a reliable marker for the net mobilization of lipid stored in heart cells. It is formed both intra- and extracellularly, and does not reflect the rate of oxidation of part of free fatty acids formed.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1435-1803
    Keywords: lipolysis ; lysosomes ; rat heart ; ischemia ; reperfusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The hormonal regulation and enzymatic basis of endogenous lipolysis in heart are not yet completely elucidated. The lysosomal fraction from rat heart appeared to be markedly enriched in triglycerides and a significant reduction in triglycerides in this fraction was found after prolonged perfusion or stimulation of lipolysis with glucagon. The enhanced rate of lipolysis, measured as glycerol release from the isolated perfused rat heart, was abolished 10–15 min after continuous glucagon administration. Omission of glucagon for another 60 min restored the ability of glucagon to stimulate lipolysis, indicating the limited availability of endogenous triglycerides and the presence of a transfer-system for triglycerides from a non-metabolically active pool to a metabolically active pool. The enhanced lipolysis induced by low-flow ischemia was found to be inhibited by the lysosomotropic agent methylamine (5 mM). Methylamine-perfusion during low-flow ischemia was accompanied by an increased recovery of myocardial triglycerides in the lysosomal fraction. The possible role of lysosome-like particles in myocardial triglyceride homeostasis was further investigated by studying the kinetics of uptake and degradation of labeled triglycerides by membrane-particles recovered in the subcellular fraction enriched with lysosomal marker enzymes. It appeared that isolated lysosomal membranes take up added triglycerides at an average rate of 30 nmoles/min/g protein. The bulk of these triglycerides taken up is stored whereas 20% is degraded to diglycerides and free fatty acids. More than 90% of the free fatty acids formed were released from the lysosomes into the supernatant. The uptake and degradation of triglyceride-filled liposomes by isolated myocardial lysosomes was inhibited during incubation with methylamine (5 mM). On the other hand, a lowering of pH during in vitro incubation increased the rate of uptake and degradation of added triglycerides by isolated lysosomes. These results indicate that lysosomes or lysosome-like particles are involved in the enhanced lipolysis during myocardial ischemia.
    Type of Medium: Electronic Resource
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