Tandem purification of two HDL-associated partner proteins in human plasma, paraoxonase (PON1) and phosphate binding protein (HPBP) using hydroxyapatite chromatography

被引：86
作者：
Renault, Frederique
Chabriere, Eric
Andrieu, Jean-Pierre
Dublet, Bernard
Masson, Patrick
Rochu, Daniel [1 ]
机构：
[1] Ctr Rech Serv Sante Armees, Unite Enzymol, Dept Toxicol, F-38702 La Tronche, France
[2] Univ Henri Poincare, CNRS, Lab Cristallog & Modelisat Mat Mineraux & Biol, F-54506 Vandoeuvre Les Nancy, France
[3] Inst Biol Struct, Lab Enzymol Mol, F-38027 Grenoble 1, France
[4] Inst Biol Struct, Lab Spectrometrie Masse Prot, F-38027 Grenoble 1, France
[5] Bundeswehr Inst Pharmacol & Toxicol, D-80937 Munich, Germany
来源：
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2006年 / 836卷 / 1-2期
关键词：
apolipoproteins; human phosphate binding protein; hydroxyapatite; organophosphates; paraoxonase;
D O I：
10.1016/j.jchromb.2006.03.029
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Human plasma paraoxonase (PON1) is calcium-dependent enzyme that hydrolyses esters, including organophosphates and lactones and exhibits anti-atherogenic properties. Human phosphate binding protein (HPBP) was discovered as contaminant during crystallization trials of PON1. This observation and uncertainties for the real activities of PON1 led us to re-evaluate the purity of PON1 preparations. We developed a hydroxyapatite chromatography for the separation of both HDL-associated proteins. We confirmed that: (1) HPBP is strongly associated to PON1 in HDL, and generally both proteins are co-purified; (2) standard purification protocols of PON1 lead to impure enzyme; (3) hydroxyapatite chromatography allows the simultaneous purification of PON1 and HPBP. (c) 2006 Elsevier B.V. All rights reserved.
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页码：15 / 21
页数：7
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