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

Autor:	Sayın M; Department of Chemistry, Science and Art Faculty, Balikesir University , Cagıs-Kampus, Balikesir , Turkey and., Guler OO
Jazyk:	angličtina
Zdroj:	Journal of enzyme inhibition and medicinal chemistry [J Enzyme Inhib Med Chem] 2015 Feb; Vol. 30 (1), pp. 69-74. Date of Electronic Publication: 2014 Mar 31.
DOI:	10.3109/14756366.2013.879578
Abstrakt:	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.
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
Nepřihlášeným uživatelům se plný text nezobrazuje	K zobrazení výsledku je třeba se přihlásit.