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Abstract
Serum paraoxonase (PON1) is a high-density lipoprotein (HDL)-associated enzyme that protects lipoproteins, both low-density lipoprotein (LDL) and HDL, against oxidation, and is considered as an antioxidative/anti-inflammatory component of HDL. In this study, PON1 was purified from bovine serum by ammonium sulfate precipitation and hydrophobic interaction chromatography on sepharose-4B-l-tyrosine-1-napthylamine. It was then immobilized on an unmodified Eupergit® C 250 L support. The immobilized PON1 retained a high catalytic activity and showed increased thermal stability compared to the native enzyme.
Acknowledgements
The authors thank Röhm GmbH & Co., Degussa (Darmstadt, Germany) for providing us with a gift of Eupergit C 250 L. They also thank Dr. Malcolm Lyon for critically reading and helpful discussion of the manuscript.
Declaration of interest
The authors have no conflicts of interest to report for this study. This work was supported by Balıkesir University Research Foundation project 2008/22.