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  • Artikel: DFG Deutsche Nationallizenzen  (4)
  • Alzheimer's disease  (2)
  • Analytical Chemistry and Spectroscopy  (2)
  • 1
    Digitale Medien
    Digitale Medien
    Presence of non-fibrillar amyloid b protein in skin biopsies of Alzheimer's disease (AD), Down's syndrome and non-AD normal persons (1994)
    Springer
    Acta neuropathologica 88 (1994), S. 201-206 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Key words Amyloid β protein ; Skin biopsy ; Alzheimer's disease ; Down's syndrome
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract A total of 66 skin biopsies from persons with Alzheimer's disease (AD) or Down's syndrome (DS) and from persons without AD were used in this study. The age range was from 7 to 89 years. Positive immunoreactivity of skin biopsies to monoclonal antibody 4G8, which is reactive to amino acid residue 17 – 24 of synthetic amyloid β protein (Aβ), and 4G8-Fab (the antigen-binding fragment of 4G8 IgG, reactive only to amyloid plaque) was observed in the epidermis-dermis junction or the basement membrane of the epidermis and in some blood vessels of the biopsy skins of 13/18 (72  %) AD, 9/10 (90  %) DS, and 14/38 (37  %) non-AD control cases. The Fisher exact probability test revealed a significant difference (P=0.0415 one-tailed) in immunoreactivity between AD and age-matched controls. There was also a significant difference (P=0.0152 one-tailed; P=0.0200 two-tailed) between DS and age-matched control in the same test. Immuno-gold electron microscopy examination of these cases with positive immunoreactivity revealed that the gold particles were deposited along the basement membrane of the epidermis. Amyloid fibrils were not observed in the regions with gold particles. Results of this study suggest that Aβ is associated with the basement membrane of skin and is present in amorphous, non-fibrillar form as soluble Aβ.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00293394
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  • 2
    Digitale Medien
    Digitale Medien
    Binding of Amyloid Beta-Protein to Intracellular Brain Proteins in Rat and Human (1998)
    Springer
    Neurochemical research 23 (1998), S. 1277-1282 
    Details
    ISSN: 1573-6903
    Schlagwort(e): Amyloid beta protein ; Alzheimer's disease ; Aβ binding proteins ; intracellular brain proteins
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Amyloid beta-protein (Aβ), in its soluble form, is known to bind several circulatory proteins such as apolipoprotein (apo) E, apo J and transthyretin. However, the binding of Aβ to intracellular proteins has not been studied. We have developed an overlay assay to study Aβ binding to intracellular brain proteins. The supernatants from both rat and human brains were found to contain several proteins that bind to Aβ 1–40 and Aβ 1–42. No major difference was observed in the Aβ binding-proteins from brain supernatants of patients with Alzheimer's disease and normal age-matched controls. Binding studies using shorter amyloid beta-peptides and competitive overlay assays showed that the binding site of Aβ to brain proteins resides between 12–28 amino acid sequence of Aβ. The presence of several intracellular Aβ-binding (AβB) proteins suggests that these proteins may either protect Aβ from its fibrillization or alternatively promote Aβ polymerization. Identification of these proteins and their binding affinities for Aβ are needed to assess their potential role in the pathogenesis of Alzheimer's disease.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1023/A:1020744216699
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  • 3
    Digitale Medien
    Digitale Medien
    Capillary end-sealing for static coating (1982)
    Weinheim : Wiley-Blackwell
    Journal of High Resolution Chromatography 5 (1982), S. 571-571 
    Details
    ISSN: 0935-6304
    Schlagwort(e): Capillary, Glass, Nylon, Teflon, Fused silica ; Static coating ; Sealing, In-place solidification ; Chemistry ; Analytical Chemistry and Spectroscopy
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Zusätzliches Material: 1 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jhrc.1240051013
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  • 4
    Digitale Medien
    Digitale Medien
    Gas chromatography of volatile fatty acids as tert-butyidimethylsilyl esters (1987)
    Weinheim : Wiley-Blackwell
    Journal of High Resolution Chromatography 10 (1987), S. 522-523 
    Details
    ISSN: 0935-6304
    Schlagwort(e): Gas chromatography ; Volatile fatty acids ; tert-Butyldimethylsilyl esters ; Chemistry ; Analytical Chemistry and Spectroscopy
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Zusätzliches Material: 1 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jhrc.1240100910
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