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  • 1
    ISSN: 0173-0835
    Keywords: Two-dimensional electrophoresis ; Serum proteins ; Acute phase ; Infectious diseases ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Acute-phase serum proteins were analyzed by two-dimensional electrophoresis with isoelectric focusing in 3-10 immobilized pH gradients. Most spots were identified by reference to the plasma map in the SWISS-2DPAGE database. Serum amyloid A protein spots were identified by immunoblotting with specific antiserum and by matching determined with predicted values of electrophoretic parameters. Changes in the concentrations of α1-antitrypsin, leucinerich glycoprotein, haptoglobin, serum retinol-binding protein and transthyretin were quantitated by densitometry of silver-stained gels. Electrophoretic patterns from 18 patients with bacterial diseases and 16 patients with viral diseases were compared. The incidence of serum amyloid A protein spots was 18/18 in bacterial diseases and 6/16 in viral diseases. As for the other reactants studied, variations were simultaneous in bacterial disease and tended to be staggered in viral diseases.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Immunoblotting ; Serum proteins ; Ampicillin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two-dimensional electrophoretograms of serum proteins from ampicillintreated patients were analyzed by immunoblotting with an antiserum specific for penicilloyl groups. As expected, human serum albumin (HSA) was the main ampicilloylated serum component. Transferrin main form II was found to be the second most important component as regards immunoblotting intensity. Immunoreactive spots were present on the acidic side of the transferrin isoelectric series, suggesting a modification mechanism similar to that observed in HSA, i.e., acylation of basic amino acid residues. Several additional ampicilloylated spots were detected but could not be assigned. Their electrophoretic parameters were determined using internal standards. This is the first description of serum proteins other than HSA being modified by ampicillin in the course of routine therapeutic treatment.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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