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  • Amyotrophic lateral sclerosis  (1)
  • Ca2+/calmodulin-dependent protein kinase II  (1)
  • Enzymeimmobilization  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Ca2+/calmodulin-dependent protein kinase II immunoreactivity in Lewy bodies (1991)
    Springer
    Acta neuropathologica 82 (1991), S. 159-163 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Lewy body ; Lewy body-like hyaline inclusion ; Ca2+/calmodulin-dependent protein kinase II ; Parkinson's disease ; Amyotrophic lateral sclerosis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00294440
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Covalent immobilization of trypsin onto poly(2-hydroxyethyl methacrylate)/polystyrene composite microspheres by cyanogen bromide method and its enzymatic activity (1987)
    Springer
    Colloid & polymer science 265 (1987), S. 957-964 
    Details
    ISSN: 1435-1536
    Schlagwort(e): Enzymeimmobilization ; trypsin ; cyanogen bromide ; emulsion ; microsphere
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie , Maschinenbau
    Notizen: Abstract Covalent immobilization of trypsin onto poly(2-hydroxyethyl methacrylate)/ polystyrene composite microspheres, produced by emulsifier-free seeded emulsion polymerization technique, was carried out using the cyanogen bromide method under various conditions. The highest enzymatic activities of the trypsin immobilized in this study against N-α-benzoyl-L-arginine ethyl ester and N-α-benzoyl-L-arginine-p-nitroanilide, as low-molecular substrates and casein as a high-molecular substrate, were high, as corresponding to 80%, 85% and 50% of those of free trypsin, respectively.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01412397
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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    Artikel (Nationallizenzen)
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