In vitro effect of ethyl acetate, butanol and water extracts of Juniperus excelsa Bieb. on angiotensin-converting enzyme purified from human plasma

Başı, Zehra; Türkoğlu, Nalân; Türkoğlu, Vedat; Karahan, Fatih

doi:10.1007/s11696-019-00806-w

Cited by 10 publications

(3 citation statements)

References 45 publications

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“…I another study the same group described sheddases able to liberate 65 and 90 kDa ACE isoforms in mesangial cells [52]. Also, in our previous studies, the molecular weight of the ACE enzyme purified from human plasma was found to be 60 and 70 kDa [53,54]. In our work, purity and molecular weight of the ACE enzyme purified from sheep lungs were designated by SDS-PAGE, and two bands, 60 kDa and 70 kDa, were observed on the gel (Figs.…”

Section: Resultsmentioning

confidence: 70%

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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Section: Resultsmentioning

confidence: 70%

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

2021

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“…In our previous study, the water and butanol phases of the Juniperus excelsa Bieb. and Matricaria chamomilla L. plants indicated an inhibition effect on ACE purified from human plasma, and IC 50 constants were 5.790, 2.858, 1.292, and 0.353 mg/mL, respectively [42,43]. In another study, the IC 50 values of two synthetic peptides TTP (Thea-Thea-Pro) and gAgAP (GABA-GABA-Pro) showing an inhibitory effect on ACE was determined as 0.92 and 3.4 μmol/L, respectively.…”

Section: Resultsmentioning

confidence: 96%

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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“…In our previous study, the water and butanol phases of the Juniperus excelsa Bieb. indicated an inhibitor impact on ACE purified from human plasma and IC 50 constants were computed to be 5.790 and 2.858 mg/mL, respectively [44]. In another study, the methanol extracts of Phyllostachys nigra and Phyllostachys pubescens bamboo shoots indicated inhibitor impact on the ACE activity and IC 50 constants were 6.0 and 3.5 mg/mL, respectively [45].…”

Section: Resultsmentioning

confidence: 99%

Investigation of inhibition effect of butanol and water extracts of Matricaria chamomilla L. on angiotensin‐converting enzyme purified from human plasma

Baş

Türkoğlu

Göz

2021

Biotech and App Biochem

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Angiotensin-converting enzyme (ACE) liable for the regulation of blood pressure was purified from human plasma by affinity chromatography. Impact of water and butanol extracts of Matricaria chamomilla L. on purity ACE was examined. ACE was purified using the affinity chromatography method. The enzyme activity was evaluated at 345 nm by a spectrophotometer. Extracts of M. chamomilla plant with butanol and water were prepared. Lisinopril was utilized as a specific inhibitor. ACE was purified 3,659-fold from human plasma and the specific activity was 1,350 EU/mg protein. The molecular weight and purity of ACE were found by SDS-PAGE and two bands of 60 and 70 kDa on the gel were detected. Water and butanol extracts of M. chamomilla demonstrated inhibitor impact on ACE activity. IC 50 constants for water and butanol extracts of M. chamomilla were computed to be 1.292 and 0.353 mg/mL, respectively. The type of inhibition for whole inhibitors was identified as noncompetitive. IC 50 and K i constants for lisinopril were calculated to be 0.781 and 0.662 nM, respectively. These results indicate that butanol and water extracts of M. chamomilla may have an ACE inhibitor potential.

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In vitro effect of ethyl acetate, butanol and water extracts of Juniperus excelsa Bieb. on angiotensin-converting enzyme purified from human plasma

Cited by 10 publications

References 45 publications

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

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

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

Investigation of inhibition effect of butanol and water extracts of Matricaria chamomilla L. on angiotensin‐converting enzyme purified from human plasma

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