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  • 1
    Electronic Resource
    Electronic Resource
    Kinetic characterization of GABA-transaminase from cultured neurons and astrocytes (1990)
    Springer
    Neurochemical research 15 (1990), S. 1073-1077 
    Details
    ISSN: 1573-6903
    Keywords: GABA-transaminase ; kinetics ; neurons ; astrocytes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The enzymatic mechanism and the kinetic parameters of GABA-transaminase extracted from cultured mouse cerebral cortex neurons and astrocytes were studied. Neuronal as well as astrocytic GABA-transaminase obeyed a bi bi ping-pong reaction mechanism. The estimated Km-values for α-ketoglutarate and GABA were significantly lower for astroglial GABA-transaminase compared to the neuronal enzyme suggesting a possible existence of cell specific isozymes of GABA-transaminase. The observed enzymatic mechanism and the magnitude of the estimated kinetic parameters imply that GABA-transaminase synthesized in the two types of cultured neural cells is mechanistically and kinetically equivalent to the enzyme synthesized in the brainin vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01101706
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Glutaminase in neurons and astrocytes cultured from mouse brain: Kinetic properties and effects of phosphate, glutamate, and ammonia (1988)
    Springer
    Neurochemical research 13 (1988), S. 383-388 
    Details
    ISSN: 1573-6903
    Keywords: Glutaminase ; neurons ; astrocytes ; phosphate ; glutamate ; ammonia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Phosphate activated glutaminase comprises two kinetically distinguishable enzyme forms in cultures of cerebellar granule cells, of cortical neurons and of astrocytes. Specific activity of glutaminase is higher in cultured neurons compared with astrocytes. Glutaminase is activated by phosphate in all cell types investigated, however, glutaminase in astrocytes reguires a much higher concentration of phosphate for half maximal activation. One of the products, glutamate, inhibits the enzyme strongly, whereas the other product ammonia has only a slight inhibitory action on the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00972489
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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