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  • Digitale Medien  (2)
  • 1995-1999  (1)
  • 1985-1989  (1)
  • 1970-1974
  • Hemidesmosome  (1)
  • Imidazole compound  (1)
Materialart
  • Digitale Medien  (2)
Erscheinungszeitraum
  • 1995-1999  (1)
  • 1985-1989  (1)
  • 1970-1974
Jahr
  • 1
    ISSN: 1438-2199
    Schlagwort(e): Amino acids ; Imidazole compound ; Mercaptopyruvic acid ; Urocanic acid ; Histidine ; Mass spectrometry ; Paper electrophoresis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary S-[2-Carboxy-1-(1H-imidazol-4-yl)ethyl]-3-mercaptopyruvic acid (I) was chemically synthesized in 15% yield by incubating a reaction mixture oftrans-urocanic acid and 3-fold excess of 3-mercaptopyruvic acid at 45°C for 6 days. The synthesized compound was characterized by fast-atom-bombardment mass spectrometry and high-voltage paper electrophoresis. CompoundI was identified with a product of an enzymatic reaction ofS-[2-carboxy-1-(1H-imidazol-4-yl)ethyl]-l-cysteine (II) with rat liver homogenate in a phosphate buffer, pH 7.4. CompoundI was degraded toS-[2-carboxy-1-(1H-imidazol-4-yl)ethyl]-3-mercaptolactic acid (III), a compound previously found in human urine [Kinuta et al. (1994) Biochem J 297: 475–478], by incubation with rat liver homogenate. From these results, we suggest that compoundI is a metabolic intermediate for the formation of compoundIII from compoundII. The present pathway follows a formation of compoundII fromS-[2-carboxy-1-(1H-imidazol-4-yl)ethyl] gluthathione [Kinuta et al. (1993) Biochim Biophys Acta 1157: 192–198], a proposed metabolite ofl-histidine.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1432-069X
    Schlagwort(e): Bullous pemphigoid antigen ; Hemidesmosome ; Immunoelectron microscopy ; Immunogold ; Cryosubstitution
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary Using low-temperature postembedding techniques for immunoelectron microscopy, we succeeded in demonstrating the precise localization of bullous pemphigoid antigen (BP-Ag) in normal human skin. Small pieces (〈1 mm3) of normal adult skin were rapidly frozen in liquid propane at-190°C and subjected to freeze substitution with 100% methanol at-80°C. Specimens were embedded in Lowicryl K11M at-60°C which was polymerized under ultraviolet radiation at-60°C. Ultrathin sections were incubated with BP sera followed by rabbit anti-human IgG and colloidal-gold conjugated anti-rabbit IgG. Epidermal ultrastructure was generally well preserved: the basal cell plasma membrane and intra- and extracellular components of hemidesmosomes could be resolved. Gold particles were mainly distributed on and around the hemidesmosomes in both intra- and extracellular sites, with most of the labelling being inside the basal keratinocytes and within about 300 nm of the basal plasma membrane. No specific labelling was observed beneath melanocytes or when normal human serum was used as a control instead of BP serum. Our observations indicate that BP-Ag is localized in and around hemidesmosomes in normal human skin and that the antigen has both intracellular and extracellular domains with the major component occurring inside the cells.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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