Stability of highly purified human paraoxonase (PON1): Association with human phosphate binding protein (HPBP) is essential for preserving its active conformation(s)-Reference-Cited by-同舟云学术

Stability of highly purified human paraoxonase (PON1): Association with human phosphate binding protein (HPBP) is essential for preserving its active conformation(s)

Published:2007-07 Issue:7 Volume:1774 Page:874-883
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Rochu Daniel,Renault Frédérique,Cléry-Barraud Cécile,Chabrière Eric,Masson Patrick

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference42 articles.

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3. The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin;Davies;Nat. Genet.,1996

4. Structure–reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase;Khersonsky;Biochemistry,2005

5. Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization;Aharoni;Proc. Natl. Acad. Sci. U. S. A.,2004

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