Purification of angiotensin‐converting enzyme from human plasma and investigation of the effect of some active ingredients isolated from <scp><i>Nigella sativa</i></scp> L. extract on the enzyme activity

Başı, Zehra; Türkoğlu, Vedat

doi:10.1002/bmc.4175

Cited by 15 publications

(5 citation statements)

References 44 publications

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“…The molecular weight of ACE purified from the ostrich (Struthio camelus) lung was detected as about 200 kDa [7]. At the same time, similar to our study, the molecular weight of ACE enzyme purified from human plasma was found as 60 and 70 kDa [38]. Two isoenzymes of the ACE were determined in the somatic form.…”

Section: Resultssupporting

confidence: 88%

Purification of Angiotensin-Converting Enzyme (ACE) from Sheep Kidney and Inhibition Effect of Reduced Nicotinamide Adenine Dinucleotide (NADH) on Purified ACE Activity

Kiylik

Türkoğlu

Baş

2021

Cell Biochem Biophys

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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 IC 50 and K i values for NADH were 244.33 and 175.08 µM, respectively. These results suggest that antioxidant substances might be efficient in preventing hypertension.

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Section: Resultssupporting

confidence: 88%

Purification of Angiotensin-Converting Enzyme (ACE) from Sheep Kidney and Inhibition Effect of Reduced Nicotinamide Adenine Dinucleotide (NADH) on Purified ACE Activity

Kiylik

Türkoğlu

Baş

2021

Cell Biochem Biophys

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“…6). Similarly, in our previous work, the optimum pH value of the ACE enzyme purified from human plasma was found between 7.4 and the optimum temperature between 35-40 °C [56]. In another work, ACE was purified from rabbit lung and the optimum temperature was 37 °C and the optimum pH was 8.0-8.3 [57].…”

Section: Resultssupporting

confidence: 62%

Purification and characterization of angiotensin-converting enzyme (ACE) from sheep lung

2021

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Angiotensin-converting enzyme (ACE, EC 3.4.15.1) in the renin-angiotensin system regulates blood pressure by catalyzing angiotensin I to the vasoconstrictor angiotensin II. In this study, the ACE was purified and characterized from sheep lung. The kinetic properties of the ACE were designated. The inhibition effect of captopril, a specific ACE inhibitor, was determined. ACE was purified from sheep lung using the affinity chromatography method in one step. NHS-activated Sepharose 4 Fast Flow as column filler and lisinopril as a ligand in this method used. The molecular weight and purity of ACE were designated using the SDS-PAGE method. Optimum temperature and optimum pH were found for purified ACE. K M and V max values from Lineweaver-Burk charts determined. The inhibition type, IC 50 , and K i values of captopril on purified ACE were identified. ACE was 6405-fold purified from sheep lung by affinity chromatography in one step and specific activity was 16871 EU/mg protein. The purity and molecular weight of ACE were found with SDS-PAGE and observed two bands at around 60 kDa and 70 kDa on the gel. Optimum temperature and optimum pH were designated for purified ACE. Optimum temperature and pH were found as 40 °C and pH 7.4, respectively. V max and K M values were calculated to be 35.59 (µmol/ min).mL −1 and 0.18 mM, respectively. IC 50 value of captopril was found as 0.51 nM. The inhibition type of captopril was determined as non-competitive from the Lineweaver-Burk graph and the K i value was 0.39 nM. As a result, it was observed in this study that the ACE enzyme can be successfully purified from sheep lungs in one step. Also, it was determined that captopril, which is a specific ACE inhibitor, has a significant inhibitory effect with a very low IC 50 value of 0.51 nM.

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“…In another study, some natural fatty oils were obtained from Nigella sativa plant and the in vitro effects of the isolated fatty acids on the enzyme activity were investigated. It was found that most of these oils showed inhibition of angiotensin‐converting enzyme (Basi & Turkoglu, ). Rašković and his co‐workers reported an essential oil mixture [1,8‐cineole (43.77%), camphor (12.53%) and α ‐pinene (11.51%)] obtained from the n ‐hexane phase of Rosmarinus officinalis (Rašković et al, ).…”

Section: Resultsmentioning

confidence: 99%

Investigation of the effects of natural compounds isolated from Arum rupicola var. rupicola on glutathione reductase enzyme purified from bovine liver

Kivanç

Türkoğlu

2019

Biomedical Chromatography

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Glutathione reductase (GR, E.C. 1.8.1.7), a flavoenzyme, is responsible for recycling of oxidized glutathione disulfide. This study was performed in two main sections. In the first GR was purified from bovine liver by affinity column chromatography and the purification rate and specific activity of the enzyme were calculated as 1832-fold and 141 EU/mg protein, respectively. The subunit molecular weight of the enzyme was determined as 55 kDa by means of SDS-PAGE. The second section isolated natural components of Arum rupicola Boiss. var. rupicola using column chromatography.The isolation protocol for this plant was performed with a series of different-sized columns with hexane-ethyl acetate. According to the thin-layer chromatography plate, seven substances (R1-R7) were isolated. Our study's aim was to find new activators or inhibitors for GR activity. With this aim, all isolated substances were tested for GR activity. R6 showed competitive inhibition, while R4 had noncompetitive inhibition of GR activity. R1 played a role as an activator of GR activity.The inhibitory activity percentage vs. concentration graph was plotted. Values of IC 50 for R4 and R6 were calculated as 0.193 mg/mL and 3.98 μg/mL, respectively, from the equation of this graph.Additional supporting information may be found online in the Supporting Information section at the end of the article. How to cite this article: Kıvanç MR, Türkoglu V. Investigation of the effects of natural compounds isolated from Arum rupicola var. rupicola on glutathione reductase enzyme purified from bovine liver. Biomedical Chromatography. 2019;33:e4560.

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Purification of angiotensin‐converting enzyme from human plasma and investigation of the effect of some active ingredients isolated from Nigella sativa L. extract on the enzyme activity

Cited by 15 publications

References 44 publications

Purification of Angiotensin-Converting Enzyme (ACE) from Sheep Kidney and Inhibition Effect of Reduced Nicotinamide Adenine Dinucleotide (NADH) on Purified ACE Activity

Purification of Angiotensin-Converting Enzyme (ACE) from Sheep Kidney and Inhibition Effect of Reduced Nicotinamide Adenine Dinucleotide (NADH) on Purified ACE Activity

Purification and characterization of angiotensin-converting enzyme (ACE) from sheep lung

Investigation of the effects of natural compounds isolated from Arum rupicola var. rupicola on glutathione reductase enzyme purified from bovine liver

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