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  • Electronic Resource  (3)
  • 2000-2004  (1)
  • 1990-1994  (2)
  • 1965-1969
  • Propranolol ester derivatives  (2)
  • De novo mutation  (1)
Material
  • Electronic Resource  (3)
Years
  • 2000-2004  (1)
  • 1990-1994  (2)
  • 1965-1969
Year
  • 1
    ISSN: 1432-0533
    Keywords: Key words Dejerine-Sottas disease ; Point mutation ; De novo mutation ; Peripheral myelin protein 22 (PMP22) ; Onion-bulb
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The Ser149Arg mutation of peripheral myelin protein 22 (PMP22) was found in a 19-year-old woman with a sporadic case of Dejerine-Sottas disease. The patient showed delayed motor development. She walked for the first time with support at the age of 2 years. Scoliosis developed at age 4 years. Her walking ability was best at age 11. Thereafter, she showed progressive muscle weakness and sensory disturbances in the distal extremities. At the age of 18 years, the use of a wheelchair became necessary. Motor and sensory nerve conduction studies showed absent motor and sensory responses on electrical stimulation of the limb nerves. A sural nerve biopsy specimen showed marked decreases in the numbers of both large and small myelinated fibers, abundant onion-bulb formation, and hypomyelination. Electron microscopic observation revealed the presence of demyelinated axons and myelin sheaths disproportionately thin relative to axon diameter. That this was a de novo mutation was established by parentage testing and PMP22 gene analysis of the parents. The mutation seems to be novel and dominant.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Chiral separation ; Alpha 1-acid glycoprotein-bonded column ; Propranolol ; Propranolol ester derivatives
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The retention, enantionselectivity and enantiomeric elution order of racemic propranolol (PP) and its ester derivatives (O-acetyl,-propionyl,-butyrul and-valeryl PP) on an α1-acid glycoprotein (AGP)-bonded column have been investigated by changing eluent composition (eluent pH, buffer concentration, type and content of organic modifier). The retention of these cationic solutes, PP and its ester derivatives, was influenced by eluent pH, ionic strength and organic modifier content. The enantioselectivity was dependent on eluent pH and type of organic modifier. Reversal of the enantiomeric elution order of ester derivatives of PP (O-propionyl-butyryl) and-valeryl PP) occurred around eluent pH 6–7. These results suggst that chiral recognition or binding properties may be altered by the change in eluent composition, espeically eluent pH and type of organic modifier.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Ovomucoid-bonded silica ; Chiral separation ; Propranolol ; Propranolol ester derivatives
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The retention, enantioselectivity and enantiomeric elution order of racemic propranolol (PP) and its ester derivatives (O-acetyl,-propyl,-butyl and-valeryl PP) on an ovomucoid-bonded silica column have been investigated with respect to pH, ionic strength and organic modifier. For these cationic solutes, an increase in the organic modifier content and/or a decrease in the pH result in a decreased retention of both enantiomers. Enantioselectivity of the ester derivatives was higher than of underivated PP. The enantiomeric elution order was (S)/(R) for PP and (R)/(S) for the four ester derivatives, when ethanol or 2-propanol was used as the organic modifier. When methanol or acetonitrile was used as the organic modifier, inversion of the enantiomeric elution order was observed for O-valeryl PP with the use of methanol and for PP and O-propyl PP with acetonitrile. These results suggest that at least two chiral binding- or recognitionsites are present in a protein molecule and/or conformational changes occur in the chiral binding- or recognition-site(s) of the protein molecule bonded to a silica matrix.
    Type of Medium: Electronic Resource
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