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  • 2015-2019  (1)
  • 1980-1984  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Occurrence and Properties of Phospholipases A1 of Plasma Membranes Prepared from Neuronal- and Glial-Enriched Fractions of the Rabbit Cerebral Cortex (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Exogenously added glycerophosphatides, specifically radioactively labelled either in the 1 or in the 2 position, were used to investigate the occurrence and properties of phospholipase A1 in plasma membranes prepared from neuronal- and glial-enriched fractions of rabbit brain. Phospholipase A1 activity was maximal at pH values ranging between 8.0 and 9.0 for the plasma membranes of both cell types. The enzyme activity was most abundant in the microsomal fraction, with a neurondglial ratio of about 2. The plasma membranes displayed about half the enzymic activity of the microsomal fraction, whereas only small amounts of phospholipase A1 were present in the neuronal and glial mitochondria. Investigations on the substrate specificity showed a different pattern for the enzyme of neuronal and glial origin. The release of labelled fatty acids from phosphatidylcholine by the neuronal plasma membrane phospholipase A1 decreased with increasing degree of unsaturation of the fatty acids at the 1 position. The presence of plasmalogens and plasmalogen precursors in the incubation mixture appreciably inhibited the hydrolysis of the corresponding diacyl compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb01675.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Action of phospholipase A2 of rabbit neuronal and glial cells on 1,2-diacyl-, 2-acyl-1-alk-1′-enyl-, and 2-acyl-1-alkyl-glycerophosphatides (1981)
    Springer
    Neurochemical research 6 (1981), S. 23-32 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Pronounced differences in the phospholipase A2 activities were found in neurons and glia, the enzyme activity being two- to threefold higher in neurons than in glial cells. Both phospholipases A2 hydrolyzed the 1,2-diacylglycerophosphatides more rapidly than the acylalkyl and acylalkenyl compounds. Choline plasmalogen and the corresponding alkyl derivative were cleaved at similar rates by the phospholipase A2 from both glia and neurons. There was a tendency by the neuronal phospholipase A2 to release arachidonic acid faster than linolenic acid from both phosphatidylcholine and ethanolamine, while arachidonic acid was removed less actively from phosphatidylethanolamine by the glial enzyme. The glial phospholipase A2 showed a lag period of 10 or 20 min. Norepinephrine, injected into the lateral ventricle of the rabbit brain, stimulated the hydrolysis of the various 1,2-diacyl-, acylalkyl-, and acylalkenyl-glycerophosphatides by the phospholipase A2 from both glia and neurons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00963902
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Investigations of the lipid metabolism of the white matter in multiple sclerosis Changes in glycero-phosphatides and lipid-splitting enzymes (1982)
    Springer
    Neurochemical research 7 (1982), S. 727-735 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Phospho- and galacto- lipids and lipidhydrolyzing enzymes have been determined in the white matter of a young patient with a subacute course of multiple sclerosis (MS). Significant changes were observed for the concentration of glycerophosphatides and the fatty acid pattern of the normal appearing with matter surrounding MS-plaques. Among the individual glycerophosphatides a significant decrease of phosphatidylserine and phosphatidylinositol was found, whereas the ethanolamine containing phosphatides showed lower figures (non significant). The fatty acid pattern of the ethanolamine-phosphatide-fraction of the diseased tissue showed a decrease of the 18∶1 and the sum of 20∶1 and 18∶3 fatty acids as compared to the normal control, whereas the highly unsaturated, long-chained fatty acids 20∶4 (arachidonic acid) and 22∶6 (docosahexaenic acid) were elevated. The measurement of lipidhydrolyzing enzymes resulted in an increased phospholipase A1 activity in the diseased tissue. The experimental data point to a decreased activity of the fatty acid elongation system in the course of MS. The decrease of the acidic glycerophosphatides might be due to the increased phospholipase A1 activity. The impaired interaction of the lipids with the basic myelin protein, as described in the present paper, might be involved in the pathogenesis of the demyelinating process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00965525
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Sauerstoff-Messung mit ZrO2-Sonden in einer MehrbrennerfeuerungVortrag von U. Dohle auf der internen Arbeitssitzung des GVC-Fachausschusses „Hochtemperaturtechnik“ am 20. Januar 1984 in Aachen. (1984)
    Weinheim : Wiley-Blackwell
    Chemie Ingenieur Technik - CIT 56 (1984), S. 849-850 
    Details
    ISSN: 0009-286X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cite.330561107
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  • 5
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    Identifying Multivalent Binding Kinetics of Precision Glycomacromolecules: A Kinetic Study Using kinITC (2015)
    Details
    Publication Date: 2020-03-11
    Description: Multivalent sugar/protein interactions are well-known to proceed through different binding modes 1-5 which in turn can be described by their binding kinetics 3-5. This study provides additional insight into the association and dissociation reaction rates of complex multivalent sugar/protein interactions. Binding kinetics of recently introduced multivalent precision glycomacromolecules 6-8 to Concanavalin A (Con A) were studied by " kinetic Isothermal Titration Calorimetry " (kinITC) 9-11. The effect of multivalency is evaluated by comparing rate constants of glycomacromolecules obtaining the same and different valency of mannose ligands and by variation of the overall backbone properties, such as hydrophilic/ hydrophoboc. In addition, binding kinetics were studied using different conformations of Con A (homodimer vs.-tetramer) and thus a different protein valency. Our results show that precision glycomacromolecule/Con A binding proceeds non-cooperatively. Further, association and dissociation rates are mainly described by intermolecular complex formation. Together with the so-called functional valency, we can discriminate between " bound " and " unbound " states for macroscopic on-and off-rates, even for such complex glycooligomer/protein systems. By comparing e.g. a mono-to a divalent glycomacromolecule for their binding to dimeric Con A, we see a lower dissociation rate for the latter. As both bind monovalently to Con A, this is a strong indication for a statistical rebinding event. Further, there is a strong dependence of multivalent binding kinetics on the ligand density of glycomacromolecules as well as the Con A conformation and thus the overall on-and off-rates.
    Language: English
    Type: conferenceobject , doc-type:conferenceObject
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