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.

No abstract

Angiotensin converting enzyme (ACE, peptidyldipeptidase A, EC 3.4.15.1) has got a significant role in the arrangement of blood pressure. ACE inhibitors usually play a part in the therapies of hypertension. Hypertension is an significant cardiovascular risk factor. The main purpose of the treatment is to reduce the incidence of hypertension. In this study, the inhibition effect of butanol and water extracts of Thymbra sintenisii Bornm. et Aznav. Subsp on angiotensin converting enzyme (ACE) activity in human plasma was investigated. ACE activity was calculated at 345 nm spectrophotometrically. Extracts of Thymbra sintenisii Bornm. et Aznav. subsp plant with water and butanol were made. The effectiveness of these extracts on ACE activity was researched. Water and butanol extracts of Thymbra sintenisii indicated inhibition impact on ACE. IC50 values for water and butanol extracts of Thymbra sintenisii was measured to be 1.696 mg mL-1 and 0.395 mg mL-1 respectively. Inhibition type for water and butanol extracts of Thymbra sintenisii from Lineweaver-Burk chart was defined to be non-competitive inhibition. Synthetic ACE inhibitors are utilized in the therapy of hypertension. On the other hand, synthetic ACE inhibitors exhibit a large number of adverse effects. Therefore, ACE inhibitors have been newly researched from native herbs. These conclusions demonstrate that water and butanol extracts of Thymbra sintenisii plant may have an ACE inhibition capacity.

Hypertension is a very important problem around the world. The inhibition of the Angiotensin-converting enzyme (ACE, EC.3.4.15.1.) is regarded as fundamental of hypertension treatment. However, synthetic ACE inhibitors have several side effects. For this reason, there are lots of studies to improve green ACE inhibitors. Therefore, this study was designed to determine the potential inhibitory effects of two members of Apiaceae, Coriandrum sativum and Chaerophyllum macropodum, on human plasma ACE. For this purpose, water extracts of the plants were used. ACE inhibition activity was detected spectrophotometrically. Both plant extracts showed an inhibitory effect on ACE activity. The obtained results showed that Coriandrum sativum and Chaerophyllum macropodum have inhibitory effects on human plasma ACE with an IC50 value of 0.7 mg/mL and 1.14 mg/mL, respectively. Lineweaver-Burk graph was used to determine the inhibition type. The inhibition types were found as reversible noncompetitive. According to the obtained results, Coriandrum sativum and Chaerophyllum macropodum are valuable functional food with ACE inhibition capacity which may be used to balance blood pressure efficiently.

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.

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.

No abstract

Inhibition of the angiotensin-converting enzyme (ACE, EC 3.4.15.1) is one of the most important hypertension treatments. Here, ACE was purified from human plasma with affinity chromatography. The purity and molecule weight of ACE were identified utilizing the SDS-PAGE and viewed in two bands at around 60 kDa and 70 kDa on the gel. KM and Vmax constants from the Lineweaver-Burk graphic were computed to be 0.6 mM and 175.44 (µmol/min).mL-1 , respectively. The effects of folic acid (vitamin B9) on purified ACE were studied. Folic acid on purified ACE demonstrated an inhibitory efficacy. The IC50 value for folic acid was calculated to be 127.94 µM. Kind of inhibitory and Ki constant for folic acid were defined. The kind of inhibitory for folic acid was found as non-competitive inhibitory. Ki constant was computed to be 226.59 µM for folic acid. In this study, it was concluded that folic acid, which shows an inhibitor efficacy on ACE, may have both therapeutic and protective impacts against hypertension.