The effects of norepinephrine on lactoperoxidase enzyme (LPO)

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Norepinephrine, a hormone and a neurotransmitter, was known as catecholamine. In the present study, we examined the inhibitory effect of norepinephrine on lactoperoxidase enzyme purified from bovine milk. Lactoperoxidase (LPO; E.C.1.11.1.7) was purified from bovine milk with three purification steps: Amberlite Cg-50 resin, CM-Sephadex C-50 ion-exchange chromatography and Sephadex G-100 gel filtration chromatography, respectively. LPO was purified with a yield of 31.5%, a specific activity of 30.33 EU/mg proteins and 20.77 purification fold. To determine enzyme purity, SDS-PAGE was performed and single band was observed. The Rz (A412/A280) value for LPO was 0.9. The effect of norepinephrine on lactoperoxidase was determined using ABTS as a chromogenic substrate. The half maximal inhibitory concentration (IC50) value norepinephrine was found to be 67.2 μM. Also, inhibition constant (Ki) for norepinephrine was found to be 62.0 μM. Norepinephrine was found as non-competitive inhibitor. © 2010 Academic Journals.

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AlanDeğerDil
dc.contributor.authorSisecioglu, Melda
dc.contributor.authorGulcin, Ilhami
dc.contributor.authorCankaya, Murat
dc.contributor.authorAtasever, Ali
dc.contributor.authorOzdemir, Hasan
dc.date.accessioned2026-10-18T20:30:54.119568066Z
dc.date.available2026-10-18T20:30:54.119568066Z
dc.date.issued2010
dc.description.abstractNorepinephrine, a hormone and a neurotransmitter, was known as catecholamine. In the present study, we examined the inhibitory effect of norepinephrine on lactoperoxidase enzyme purified from bovine milk. Lactoperoxidase (LPO; E.C.1.11.1.7) was purified from bovine milk with three purification steps: Amberlite Cg-50 resin, CM-Sephadex C-50 ion-exchange chromatography and Sephadex G-100 gel filtration chromatography, respectively. LPO was purified with a yield of 31.5%, a specific activity of 30.33 EU/mg proteins and 20.77 purification fold. To determine enzyme purity, SDS-PAGE was performed and single band was observed. The Rz (A412/A280) value for LPO was 0.9. The effect of norepinephrine on lactoperoxidase was determined using ABTS as a chromogenic substrate. The half maximal inhibitory concentration (IC50) value norepinephrine was found to be 67.2 μM. Also, inhibition constant (Ki) for norepinephrine was found to be 62.0 μM. Norepinephrine was found as non-competitive inhibitor. © 2010 Academic Journals.
dc.identifier.endpage1356
dc.identifier.issn1992-2248
dc.identifier.issue11
dc.identifier.scopus2-s2.0-77954400476
dc.identifier.startpage1351
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/16071
dc.identifier.volume5
dc.language.isoen
dc.relation.ispartofScientific Research and Essays
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectEnzyme purification
dc.subjectInhibition
dc.subjectLactoperoxidase
dc.subjectLPO
dc.subjectNoradrenaline
dc.subjectNorepinephrine
dc.subjectBovinae
dc.titleThe effects of norepinephrine on lactoperoxidase enzyme (LPO)
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus38
rdl.source.indexSCOPUS