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  • 1970-1974  (4)
  • 1955-1959  (1)
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  • 1
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Glial cells isolated from rabbit cerebral cortex contained approximately one-third more phospholipids per unit protein than the neuronal cell bodies. The pattern of individual phospholipids was rather similar in both cell types. The incorporation of intracisternally administered 32P into neuronal and glial phospholipid classes of rabbit brain was studied at intervals ranging from 5 to 60min. In general, for all investigated phospholipids the incorporation of the label was somewhat faster in neurons than in glial cells. Phosphatidylinositol showed the fastest and ethanolamine plasmalogen the slowest incorporation of 32P in both neurons and glial cells. A lag phase of about 10 min could be observed before labelling of the glial phosphatidylcholine, phosphatidylethanolamine, ethanolamine plasmalogen, phosphatidylserine and sphingomyelin had occurred. Among the neuronal phospholipids a lag phase was found only for the labelling of the ethanolamine plasmalogen. Norepinephrine increased the incoropration of 32P into phosphatidylinositol of both glia and neurons but had no effect on the specific radioactivity of ethanolamine plasmalogen and sphingomyelin. Labelling of phosphatidylcholine was slightly inhibited in both cell types by the administration of norepinephrine.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 21 (1973), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The de novo synthesis of phosphatidylcholine and phosphatidylethanolamine in isolated neuronal and glial cells from adult rabbit brain cortex was investigated in vitro, using labelled phosphorylcholine (phosphorylethanolamine) or cytidine-5′-phosphate choline (cytidine-5′-phosphate ethanolamine), as lipid precursors. Synthesis of phospholipid from phosphorylcholine and phosphorylethanolamine in both fractions was extremely low when compared to that derived from the corresponding cytidine nucleotides. The neuronal cell-enriched fraction was found to possess a much higher rate of synthesis of both lipids from all precursors. Neuronal/glial ratios of about 5–9 were found for the synthesis of phosphatidylcholine and phosphatidylethanolamine from cytidine-5′-phosphate choline and cytidine-5′-phosphate ethanolamine, respectively. Several kinetic properties of the choline-phosphotransferase (EC 2.7.8.2) and ethanolaminephosphotransferase (EC 2.7.8.1) were found to be similar both in neurons and in glia (e.g. Km of cytidine-5′-phosphate ethanolamine, Km of diacyl glycerol, pH optimum, need for divalent cations), but the Km value for cytidine-5′-phosphate choline in glial cells was much lower (2.3 × 10−4m) than in neurons (1 × 10−3m). The Kmfor cytidine-5′-phosphate ethanolamine in both cells was much lower than in whole brain microsomes. It is concluded that the cytidine-dependent enzymic system for phosphatidylcholine and phosphatidylethanolamine synthesis is concentrated mostly in the neuronal cells, as compared to glia.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —1,2-Diacyl-, 1-alk-1′-enyl-2-acyl-and 1-alkyl-2-acyl-sn-glycero-3-phosphorylcholine, specifically labelled with different fatty acids at the 2 position, were prepared enzymically using the acyltransferase system of rabbit sarcoplasmic reticulum. The substrates were submitted to hydrolysis by mitochondrial phospholipase A2 (phosphatide acyl-hydrolase, EC 3.1.1.4) obtained from normal and from rat brain afflicted with EAE. In the acute stage of the disease an increase of approximately 25 per cent in phospholipase A 2 activity could be observed in comparison to that from the control animals for all investigated substrates. Phospholipase A2 obtained from normal rat brains and from those afflicted with EAE had a higher affinity for 1,2-diacyl-sn-glycero-3-phosphorylcholine when compared to the corresponding alkyl acyl- and alkenyl acyl-analogues. Choline plasmalogen was cleaved more slowly than the corresponding alkyl acyl derivative. The enzyme activity returned to the control level in the recovery stage of the demyelinating disease.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 23 (1974), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —The activity of phospholipase A1 (phosphatide acylhydrolase, EC 3.1.1.4) was measured against phosphatidylcholine, -ethanolamine and -serine, specifically labelled with different fatty acids at either the 1 or 2 position, during experimental allergic encephalomyelitis in rats. In the acute stage of the disease there was a significant increase in enzyme activity in comparison to that from the control animals. The enhanced phospholipase A1 activity was of the-same order of magnitude for all 1,2-diacyl-glycerophospholipids investigated. The phospholipase A1-catalysed release of labelled fatty acids from molecular species of phosphatidylcholine decreased slightly with increasing degree of unsaturation of the fatty acids at the 1-position. The Km-values of the highly purified enzyme were not altered by the demyelinating disorder. The phospholipase A1 activity returned to the control level in the recovery stage.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 71 (1959), S. 775-775 
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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