Binding properties of human albumin modified by covalent binding of penicillin.
Derivatisation of lysine residues in human albumin was performed in vitro by reaction with penicillin G. This modification reaction has been reported to occur in patients treated with high dosages of the antibiotic. The structure of the modified protein was characterised by mass spectrometry and circular dichroism. The number of the lysine residues involved depends on the time of incubation and on the drug/protein molar ratio. The secondary structure of the modified protein does not change significantly with respect to the native protein. Furthermore, the binding properties of the modified albumin were characterised by CD spectroscopy. Phenylbutazone, diazepam and bilirubin, known to bind to specific binding areas, were used as markers. A decrease of the affinity to the high-affinity binding sites was observed after the modification.
Bertucci
C
C
Centro Studio C.N.R. Macromolecole Stereoordinate ed Otticamente Attive, Dipartimento di Chimica e Chimica Industriale, Università di Pisa, via Risorgimento 35, 56126, Pisa, Italy.
Barsotti
M C
MC
Raffaelli
A
A
Salvadori
P
P
D000418:Albumins / Q000737:chemistry / Q000378:metabolism*; D002942:Circular Dichroism; D006801:Humans; D008239:Lysine / Q000378:metabolism; D013058:Mass Spectrometry; D010400:Penicillin G / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D000418:Albumins; D011994:Recombinant Proteins; D008239:Lysine; D010400:Penicillin G