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Two‐dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment
Author(s) -
Magi Barbara,
Marzocchi Barbara,
Bini Luca,
Cellesi Carla,
Rossolini Aldo,
Pallini Vitaliano
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.11501601198
Subject(s) - transferrin , isoelectric focusing , chemistry , antiserum , isoelectric point , blood proteins , electrophoresis , serum albumin , albumin , human serum albumin , chromatography , biochemistry , biology , enzyme , antibody , immunology
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.