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  • 1
    Electronic Resource
    Electronic Resource
    Ca^2^+, calmodulin-dependent phosphorylation of glycogen synthase by a brain protein kinase
    Amsterdam : Elsevier
    FEBS Letters 161 (1983), S. 28-29 
    Details
    ISSN: 0014-5793
    Keywords: Brain ; Ca^2^+ ; Calmodulin-dependent protein kinase ; Glycogen synthase ; Protein phosphorylation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(83)80723-6
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Ca2+/calmodulin-dependent protein kinase II immunoreactivity in Lewy bodies (1991)
    Springer
    Acta neuropathologica 82 (1991), S. 159-163 
    Details
    ISSN: 1432-0533
    Keywords: Lewy body ; Lewy body-like hyaline inclusion ; Ca2+/calmodulin-dependent protein kinase II ; Parkinson's disease ; Amyotrophic lateral sclerosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) is one of the predominant protein kinases in the brain. We found that CaM kinase II immunoreactivity was concentrated in the peripheral halos of Lewy bodies (LBs) in Parkinson's disease and Lewy body-like hyaline inclusions (LBHIs) in amyotrophic lateral sclerosis. An immunoelectron microscopic examination of LBs revealed that the filaments at the periphery of LBs were decorated with immunopositive deposits. Since CaM kinase II has a broad substrate specificity and can phosphorylate neurofilaments and other cytoskeletal proteins, it may play some role in the formation of LBs and LBHIs through the aberrant phosphorylation of the cytoskeletal elements in these inclusions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00294440
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Determination of reduced-form glutathione and total glutathione in blood and plasma by high performance liquid chromatography with on-column fluorescence derivatization (1998)
    Springer
    Chromatographia 48 (1998), S. 690-694 
    Details
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; On-column fluorescence derivatization ; Blood and plasma ; Glutathione ; ortho-Phthalaldehyde
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary An on-column fluorometric derivatization method has been developed for the determination of reduced-form glutathione and total glutathione in blood and plasma by high-performance liquid chromatography. Blood hemolysate or diluted plasma was deproteinized with percholoric acid. For total glutathione determination, any oxidized forms of glutathione in samples were converted to reduced-form glutathione with dithiothreitol prior to protein precipitation. Deproteinized samples were injected without pretreatment. Glutathione was fluorescence-derivatized and separated on a C18-bonded vinyl alcohol polymer column withortho-phthalaldehyde in sodium borate buffer-acetonitrile, as mobile phase; theortho-phthalaldehyde-glutathione, fluorescent isoindole adduct is measured by its fluorescence response. Due to the high sensitivity, selectivity reproducibility and the simple HPLC system, the method is particularly suitable for routine assay of numerous or small amounts of samples.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02467600
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    Paper (German National Licenses)
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