Binding properties of human albumin modified by covalent binding of penicillin

被引：12

作者：

Bertucci, C ^{[1
]}

Barsotti, MC ^{[1
]}

Raffaelli, A ^{[1
]}

Salvadori, P ^{[1
]}

机构：

[1] Univ Pisa, Dipartimento Chim & Chim Ind, Ctr Studio Macromol Stereoordinate & Otticamente, CNR, I-56126 Pisa, Italy

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2001年 / 1544卷 / 1-2期

关键词：

modified human albumin; penicillin G; protein binding; mass spectrometry; circular dichroism;

D O I：

10.1016/S0167-4838(00)00253-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：386 / 392

页数：7

共 36 条

[1]

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[2]

ASCOLI G, 1995, J PHARM SCI, V84, P137

[3]

PENICILLIN ALLERGY - FORMATION OF PENICILLOYL DETERMINANT [J].