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Purification of Angiotensin-Converting Enzyme (Ace) From Sheep Kidney and Inhibition Effect of Reduced Nicotinamide Adenine Dinucleotide (Nadh) on Purified Ace Activity

dc.authorid Bas, Zehra/0000-0002-4071-9744
dc.authorscopusid 57290455600
dc.authorscopusid 55925236900
dc.authorscopusid 57221676721
dc.contributor.author Kiylik, Aysenur
dc.contributor.author Turkoglu, Vedat
dc.contributor.author Bas, Zehra
dc.date.accessioned 2025-05-10T17:14:58Z
dc.date.available 2025-05-10T17:14:58Z
dc.date.issued 2022
dc.department T.C. Van Yüzüncü Yıl Üniversitesi en_US
dc.department-temp [Kiylik, Aysenur; Turkoglu, Vedat] Van YuzuncuYil Univ, Fac Sci, Dept Chem, Van, Turkey; [Bas, Zehra] Van Yuzuncu Yil Univ, Fac Hlth Sci, Dept Nutr & Dietet, Van, Turkey en_US
dc.description Bas, Zehra/0000-0002-4071-9744 en_US
dc.description.abstract Angiotensin-converting enzyme (ACE, EC 3.4.15.1) is a significant enzyme that regulates blood pressure. ACE inhibitors are often used in the treatment of hypertension. In this work, ACE was purified and characterized in one step with affinity chromatography from sheep kidneys. ACE was 10305-fold purified and specific activity was 19,075 EU/mg protein. The molecular weight and purity of ACE were found with SDS-PAGE and observed two bands at about 60 kDa and 70 kDa on the gel. The effects of reduced nicotinamide adenine dinucleotide (NADH), an antioxidant compound, on purified ACE activity were also researched. NADH on ACE activity showed an inhibition effect. The inhibition type of NADH was determined to be non-competitive inhibition by the Lineweaver-Burk chart and IC50 and K-i values for NADH were 244.33 and 175.08 mu M, respectively. These results suggest that antioxidant substances might be efficient in preventing hypertension. en_US
dc.description.sponsorship Van Yuzuncu Yl University [FYL-2018-7037] en_US
dc.description.sponsorship This work received financial support from the Head of Scientific Research Projects of Van Yuzuncu Yl University (FYL-2018-7037). en_US
dc.description.woscitationindex Science Citation Index Expanded
dc.identifier.doi 10.1007/s12013-021-01036-2
dc.identifier.endpage 122 en_US
dc.identifier.issn 1085-9195
dc.identifier.issn 1559-0283
dc.identifier.issue 1 en_US
dc.identifier.pmid 34618304
dc.identifier.scopus 2-s2.0-85116779612
dc.identifier.scopusquality Q3
dc.identifier.startpage 115 en_US
dc.identifier.uri https://doi.org/10.1007/s12013-021-01036-2
dc.identifier.uri https://hdl.handle.net/20.500.14720/8497
dc.identifier.volume 80 en_US
dc.identifier.wos WOS:000705751000001
dc.identifier.wosquality Q3
dc.language.iso en en_US
dc.publisher Humana Press inc en_US
dc.relation.publicationcategory Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı en_US
dc.rights info:eu-repo/semantics/closedAccess en_US
dc.subject Angiotensin-Converting Enzyme (Ace) en_US
dc.subject Reduced Nicotinamide Adenine Dinucleotide (Nadh) en_US
dc.subject Antioxidant en_US
dc.subject Purification en_US
dc.subject Inhibition en_US
dc.title Purification of Angiotensin-Converting Enzyme (Ace) From Sheep Kidney and Inhibition Effect of Reduced Nicotinamide Adenine Dinucleotide (Nadh) on Purified Ace Activity en_US
dc.type Article en_US

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