<?xml version="1.0" encoding="UTF-8"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-10-19T01:07:57Z</responseDate><request verb="GetRecord" identifier="oai:ebyu-rdlopen.rawdatalibrary.net:ebyu/15694" metadataPrefix="oai_dc">https://ebyu-rdlopen.rawdatalibrary.net/oai/request</request><GetRecord><record><header><identifier>oai:ebyu-rdlopen.rawdatalibrary.net:ebyu/15694</identifier><datestamp>2026-10-18T20:39:13Z</datestamp><setSpec>openaire</setSpec><setSpec>driver</setSpec><setSpec>com_ebyu_10000</setSpec><setSpec>col_ebyu_10001</setSpec></header><metadata><oai_dc:dc xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd"><dc:title>The inhibitory effects of L-adrenaline on lactoperoxidase enzyme purified from bovine milk</dc:title><dc:creator>Şisecioglu, Melda</dc:creator><dc:creator>Gülçin, Ilhami</dc:creator><dc:creator>Çankaya, Murat</dc:creator><dc:creator>Ozdemir, Hasan</dc:creator><dc:subject>Enzyme purification</dc:subject><dc:subject>Inhibition</dc:subject><dc:subject>L-Adrenaline</dc:subject><dc:subject>Lactoperoxidase</dc:subject><dc:subject>Bovinae</dc:subject><dc:subject>Biology</dc:subject><dc:subject>Colloids</dc:subject><dc:subject>Dextran</dc:subject><dc:subject>Gel permeation chromatography</dc:subject><dc:subject>Ion exchange</dc:subject><dc:subject>Mammals</dc:subject><dc:subject>Purification</dc:subject><dc:subject>Amberlite CG-50</dc:subject><dc:subject>Bovine milk</dc:subject><dc:subject>Chromogenic substrate</dc:subject><dc:subject>Gel-filtration chromatography</dc:subject><dc:subject>Inhibition constants</dc:subject><dc:subject>Inhibitory concentration</dc:subject><dc:subject>Inhibitory effect</dc:subject><dc:subject>Living organisms</dc:subject><dc:subject>Physiological process</dc:subject><dc:subject>SDS-PAGE</dc:subject><dc:subject>Sephadex</dc:subject><dc:subject>Single band</dc:subject><dc:subject>Specific activity</dc:subject><dc:subject>Enzyme inhibition</dc:subject><dc:description>L-Adrenaline belongs to a group of compounds known as catecholamines, which play an important role in the regulation of the physiological process in living organisms. In the present study, the inhibitory effect of L-adrenaline on lactoperoxidase was examined. Lactoperoxidase (E.C.1.11.1.7) was purified from bovine milk with three consecutive steps: Amberlite CG-50 resin, CM-Sephadex C-50 ion-exchange, and Sephadex G-100 gel filtration chromatography. Lactoperoxidase was purified with a yield of 42.18%, a specific activity of 30.33 EU/mg proteins, and 20.77 purification fold. Enzyme purity was determined with SDS-PAGE, where a single band was observed. The Rz (A 412/A280) value for lactoperoxidase was 0.9. The effect of L-adrenaline on lactoperoxidase was determined using ABTS as a chromogenic substrate. The half maximal inhibitory concentration (IC50) value and an inhibition constant (Ki) values for L-adrenaline were 34.5 and 2.26 μM, respectively. L-Adrenaline was found to be a non-competitive inhibitor. Copyright © Taylor &amp; Francis Group, LLC.</dc:description><dc:publisher>TAYLOR &amp; FRANCIS INC</dc:publisher><dc:date>2012</dc:date><dc:type>Article</dc:type><dc:identifier>https://rdlopen.rawdatalibrary.net/r/ebyu/15694</dc:identifier><dc:identifier>https://doi.org/10.1080/10942912.2010.511924</dc:identifier><dc:identifier>1532-2386</dc:identifier><dc:language>en</dc:language><dc:relation>International Journal of Food Properties</dc:relation><dc:rights>info:eu-repo/semantics/openAccess</dc:rights><dc:type>info:eu-repo/semantics/article</dc:type><dc:identifier>https://ebyu-rdlopen.rawdatalibrary.net/tr/items/ebyu/15694</dc:identifier></oai_dc:dc></metadata></record></GetRecord></OAI-PMH>