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  • Electronic Resource  (3)
  • 1995-1999  (2)
  • 1990-1994  (1)
  • 1980-1984
  • 1960-1964
  • Magnetic resonance imaging  (2)
  • Acclimation  (1)
Material
  • Electronic Resource  (3)
Years
  • 1995-1999  (2)
  • 1990-1994  (1)
  • 1980-1984
  • 1960-1964
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Neuroradiology 38 (1996), S. 466-467 
    ISSN: 1432-1920
    Keywords: Cervical chordoma ; Magnetic resonance imaging ; Computed tomography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We report CT and MRI findings of an unusual cervical chordoma. CT showed only minimal bony destruction with a lobulated prevertebral mass. Sagittal MRI, however, clearly demonstrated a lesion involving the body of C2 extending prevertebrally and into the spinal canal.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Neuroradiology 38 (1996), S. 466-467 
    ISSN: 1432-1920
    Keywords: Key words Cervical chordoma ; Magnetic resonance imaging ; Computed tomography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We report CT and MRI findings of an unusual cervical chordoma. CT showed only minimal bony destruction with a lobulated prevertebral mass. Sagittal MRI, however, clearly demonstrated a lesion involving the body of C2 extending prevertebrally and into the spinal canal.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    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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