Binding properties of human albumin modified by covalent binding of penicillin.
作者： Carlo Bertucci , Maria Chiara Barsotti , Andrea Raffaelli , Piero Salvadori
DOI: 10.1016/S0167-4838(00)00253-3
关键词: Albumin 、 Plasma protein binding 、 Protein G 、 Biochemistry 、 Lysine 、 Circular dichroism 、 Binding site 、 Chromatography 、 Penicillin 、 Protein secondary structure 、 Chemistry
摘要: Derivatisation of lysine residues in human albumin was performed vitro by reaction with penicillin G. This modification has been reported to occur patients treated high dosages the antibiotic. The structure modified protein characterised mass spectrometry and circular dichroism. number involved depends on time incubation drug/protein molar ratio. secondary does not change significantly respect native protein. Furthermore, binding properties were CD spectroscopy. Phenylbutazone, diazepam bilirubin, known bind specific areas, used as markers. A decrease affinity high-affinity sites observed after modification.
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