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牛血清对氧磷酶的纯化及其通过共价连接固定于Eupergit C 250 L上。

Purification of bovine serum paraoxonase and its immobilization on Eupergit C 250 L by covalent attachment.

作者信息

Sayın Murat, Guler Ozen Ozensoy

机构信息

Department of Chemistry, Science and Art Faculty, Balikesir University , Cagıs-Kampus, Balikesir , Turkey and.

出版信息

J Enzyme Inhib Med Chem. 2015 Feb;30(1):69-74. doi: 10.3109/14756366.2013.879578. Epub 2014 Mar 31.

DOI:10.3109/14756366.2013.879578
PMID:24679050
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.

摘要

血清对氧磷酶(PON1)是一种与高密度脂蛋白(HDL)相关的酶,可保护低密度脂蛋白(LDL)和HDL等脂蛋白免受氧化,被认为是HDL的一种抗氧化/抗炎成分。在本研究中,通过硫酸铵沉淀和在琼脂糖-4B-L-酪氨酸-1-萘胺上的疏水相互作用色谱法从牛血清中纯化出PON1。然后将其固定在未修饰的Eupergit® C 250 L载体上。与天然酶相比,固定化的PON1保留了较高的催化活性并表现出更高的热稳定性。

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