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  • Chemistry  (1)
  • Short-chain acyl-CoA dehydrogenase deficiency  (1)
  • 1
    ISSN: 1432-1076
    Keywords: Key words Mitochondrial fatty acid oxidation ; Short-chain acyl-CoA dehydrogenase deficiency ; Ethylmalonic aciduria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Two HLA-identical twin sisters are reported, of whom one has remained essentially asymptomatic, and an episode of hypotonia and decreased level of conciousness being the only relevant clinical finding in the other. Organic acid analysis revealed that ethylmalonate was constantly, although sometimes only slightly, increased. No abnormal acylglycines or acylcarnitines could be detected. Enzyme assay in cultured skin fibroblasts confirmed short-chain acyl-CoA dehydrogenase deficiency. Conclusion The lack of appropriate biochemical markers for this deficiency makes the diagnosis difficult and consequently, the low number of patients described may be the result of underdiagnosis.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Polymer International 39 (1996), S. 17-30 
    ISSN: 0959-8103
    Keywords: Membrane ; microfiltration ; poly(vinylidene difluoride) ; alkaline phosphatase ; immobilization ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Alkaline phosphatase from human placenta has been chemically immobilized on a hydrophilic cross-flow microfiltration membrane made from poly(vinylidene difluoride) (PVDF) derivatized with 1,1′-carbonyldiimidazole. The physicochemical characterization of the immobilized biocatalyst paid special attention to the irreversibility of the bonding of the enzyme to the support, the effects of pH, temperature and ionic strength on this activity, the existence of limitations of internal and external diffusion for H+, substrate and/or products, and the kinetic behavior (intrinsic and/or effective) of the immobilized enzyme. With respect to enzyme stability, patterns of hysteresis or memory are proposed, to account for a catalytic activity affected by previous experimental events and situations. The intrinsic kinetic behaviour, rate versus substrate concentration in the absence of diffusional restrictions, was analysed graphically and numerically (by non-linear regression and by utilizing the F statistical test for model discrimination), postulating a minimum rational rate equation of 2:2 degree in substrate concentration. In concordance, a mechanistic kinetic scheme for the catalytic enzyme action has been postulated.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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