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  • Electronic Resource  (3)
  • 1990-1994  (3)
  • Propranolol  (2)
  • Endothelin  (1)
  • 1
    ISSN: 1432-0428
    Keywords: Endothelin ; radioimmunoassay ; diabetes mellitus ; fast protein liquid chromatography ; endothelial cell ; angiopathy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Plasma concentrations of endothelin, a vasoconstrictor peptide released from vascular endothelial cells, have been measured by radioimmunoassay in 100 patients with diabetes mellitus and 19 healthy subjects. The plasma immunoreactive-endothelin concentrations were found to be greatly raised in the patients with diabetes (1,880±120 fmol/l, mean±SEM) compared with the healthy subjects (540±50 fmol/l, p〈0.005). The elevation of immunoreactive-endothelin could not be explained by secondary changes in blood pressure or renal disease and did not correlate with the presence of diabetic retinopathy, duration of diabetes mellitus, fasting blood glucose or serum fructosamine. Fast protein liquid chromatographic analysis of the diabetic plasma immunoreactive-endothelin showed three forms, one in a very big molecular weight position, one intermediate and one in the position of endothelin-1 itself. No material appeared in the positions of endothelin-2 and 3. Chromatographic analysis of normal plasma showed only the big molecular weight peak while material in the endothelin-1,2 or 3 positions was below detection. The elevation of endothelin in diabetic patients may be a marker of, and further exacerbate, their vascular disease.
    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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