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  • Articles: DFG German National Licenses  (2)
  • Electronic Resource  (2)
  • 1990-1994  (1)
  • 1985-1989  (1)
  • 1955-1959
  • ATPase activity  (1)
  • Antikeratin autoantibodies  (1)
Source
  • Articles: DFG German National Licenses  (2)
Material
  • Electronic Resource  (2)
Years
  • 1990-1994  (1)
  • 1985-1989  (1)
  • 1955-1959
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 281 (1989), S. 377-382 
    ISSN: 1432-069X
    Keywords: Lichen amyloidosus ; Macular amyloidosis ; Antikeratin autoantibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In order to characterize immunoglobulins found on amyloid deposits of lichen amyloidosus and macular amyloidosis, an elution from cryostat sections was performed with citrate buffer, glycine buffer, NaCl, and PBS. Resulting eluates (mainly IgG) were examined with dot immunoblotting and SDS-PAGE immunoblotting and were found to react with the human epidermal keratin of 50 and 67 kD. Antikeratin autoantibody activities in normal murine and human sera were examined using a dot immunoblotting assay. In murine sera, titers of IgG and IgM autoantibodies were higher in older mice. The human cord blood showed significantly lower IgM autoantibody titers, whereas IgG antibody titers showed no significant differences from adults' sera, probably due to the permeability of IgG through the placental barrier. A stronger antibody activity in older individuals was thought to be due to the repeated exposures to keratin proteins derived from apoptotic keratinocytes. Sera from lichen amyloidosus and macular amyloidosis patients did not show any difference from normal controls in their antikeratin titers. It was concluded that the patients with lichenoid or macular amyloidosis are capable of producing a normal level of antikeratin autoantibodies. However, the removal of opsonized keratin-type amyloid from the skin is slow or deficient due to as yet unknown factors.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 160 (1990), S. 233-239 
    ISSN: 1432-136X
    Keywords: Temperature ; Acclimation ; Myosin ; Myosin heavy chain ; ATPase activity ; Carp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Myosins were isolated from dorsal ordinary muscles of carp acclimated to 10°C and 30°C for a minimum of 5 weeks and examined for their ATPase activities. Ca2+-ATPase activity was different between myosins from cold-and warm-acclimated carp, especially at KCl concentrations ranging from 0.1 to 0.2 M, when measured at pH 7.0. The highest activity was 0.32 μmol Pi·min-1·mg-1 at 0.2 M KCl for cold-acclimated carp and 0.47 μmol Pi·min-1·mg-1 at 0.1 M KCl for warm-acclimated fish. The pH-dependency of Ca2+-ATPase activity at 0.5 M KCl for both carp was, however, similar exhibiting two maxima around 0.3 μmol Pi·min-1·mg-1 at pH 6 and 0.4 μmol Pi·min-1·mg-1 at pH 9. K+(EDTA)-ATPase activity at pH 7.0 neither exhibited differences between both myosins. It increased with increasing KCl concentration showing the highest value of about 0.4 μmol Pi·min-1·mg-1 at 0.6–0.7 M KCl. Actin-activated myosin Mg2+-ATPase activity was markedly different between cold-and warm-acclimated carp. The maximum initial velocity was 0.53 μmol Pi·min-1·mg-1 myosin at pH 7.0 and 0.05 M KCl for cold-acclimated carp, which was 1.6 times as high as that for warm-acclimated carp. These differences were in good agreement with those obtained with myofibrillar Mg2+-ATPase activity between both carp. No differences were, however, observed in myosin affinity to actin. Differences in myosin properties between cold- and warm-acclimated carp were further evidenced by its thermal stability. The inactivation rate constant of myosin Ca2+-ATPase was 25·10-4·s-1 at 30°C and pH 7.0 for cold-acclimated carp, which was about 4 times as high as that for warm-acclimated carp. Light chain composition did not differ between both carp myosins. The differences in a primary structure of the heavy chain subunit was, however, clearly demonstrated between both myosins by peptide mapping.
    Type of Medium: Electronic Resource
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