Assay of angiotensin I-converting enzyme-inhibiting activity based on the detection of 3-hydroxybutyric acid

Lam, Le Hoang; Shimamura, Takeshi; Sakaguchi, Ken; Noguchi, Katsuya; Ishiyama, Munetaka; Fujimura, Yume; Ukeda, Hiroyuki

doi:10.1016/j.ab.2007.02.017

Cited by 27 publications

(19 citation statements)

References 11 publications

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“…This method is very useful and highly sensitive as it uses a visible light microplate reader (Lam le et al, 2007(Lam le et al, , 2008. Briefly, diluted samples were placed into the wells of a 96-well microplate, and the enzyme mixture was added to each well.…”

Section: Methodsmentioning

confidence: 99%

Inhibition of Angiotensin-Converting Enzyme by Components of Traditional Mongolian Fermented Milk Products

Bayarsaikhan

Ohnishi‐Kameyama

Shirai

et al. 2011

FSTR

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Several angiotensin-converting enzyme (ACE) inhibitory peptides have been detected in milk products. There are many traditional milk products in Mongolia. For this study, some Mongolian milk products were collected, and the ACE inhibitory activities of these samples were tested; an active fraction was found in aaruul made from mare's milk. After purification by dialysis and HPLC, the active fractions were isolated. The molecular weight of the active component was 362.05 M, as determined by mass spectrometry. An authentic standard was used to determine the IC 50 value of the inhibitory activity. From the results of molecular weight, the active component in aaruul was identified as 5′-GMP. The activity of 5′-GMP is not much higher than that of the active peptide in sour milk and some flavonoids. However, this is the first report that shows that 5′-GMP inhibits ACE activity. These results will provide useful information for the development of hypertension therapy agents.

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Section: Methodsmentioning

confidence: 99%

Inhibition of Angiotensin-Converting Enzyme by Components of Traditional Mongolian Fermented Milk Products

Bayarsaikhan

Ohnishi‐Kameyama

Shirai

et al. 2011

FSTR

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“…This will cause a disruption in ACE activity absorption so that the result was not specific. 10 Therefore, ACE activity test method was conducted using the kit because this method was more sensitive, accurate, and fast compared with the conventional method.…”

Section: Ace Inhibition Activity Testmentioning

confidence: 99%

Inhibition Activity of Angiotensin Converting Enzyme (ACE) and Determination of Total Phenolic and Flavonoid Compound from Bitter Melon Leaves (Momordica charantia L.)

Lestari¹,

Katrin²,

Rissyelly³

et al. 2017

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Introduction: Hypertension is a leading problem in Indonesia, because of the high prevalence and the long term effect. Bitter melon leaves (Momordica charantia L.) has been traditionally utilized to treat hypertension, yet not many studies explained the antihypertension effect of this plant. Methods: This study was conducted to test the benefit of bitter melon leaves as antihypertension using angiotensin converting enzyme inhibition activity in 80% ethanolic extract and its fractions (n-hexane, ethyl acetate, and n-butanol) using ACE kit-WST (Dojindo, Japan). Then the antihypertension activity was associated with the phenolic content which was expressed in gallic acid equivalent (GAE) and total flavonoid in quercetin equivalent (QE). Results: Result of the study showed that the IC50 value obtained from the ethanolic extract to inhibit ACE activity was 7.52 μg/mL and the highest inhibition obtained in ethyl acetate fraction with IC50 value was 4,29 μg/mL. Phenolic total and flavonoid total determination also showed that the highest content obtained in ethyl acetate fraction with 18.752 mg GAE/gr extract and 8.310 mg QE/gr extract, respectively. Conclusion: According to the study, it could be concluded that bitter melon (Momordica charantia L.) leaves provide inhibition activity against Angiotensin Converting Enzyme (ACE) and chemical compounds that were expected to play an active role in inhibiting ACE were flavonoid and tannin.

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“…2 Briefly, the enzymatic reaction was initiated by the additions of 50 ml of 0. 15 ml of an ACE inhibitor.…”

Section: Generation Of 3hb From 3hb-ggg and Detection Of 3hb Using Anmentioning

confidence: 99%

“…3HB-GGG was synthesized according to our previous report. 2 The F-kit was purchased from R-Biopharm (Darmstadt, Germany). ACE inhibitory drinks (Tokuho), including Tokuho A (0.034 mg ml -1 of Ile-Pro-Pro and Val-ProPro), Tokuho B (0.004 mg ml -1 of Val-Tyr), and Tokuho C (0.002 mg ml -1 of Val-Tyr), were purchased from local supermarkets.…”

Section: Reagents and Chemicalsmentioning

confidence: 99%

“…The proposed assay was more sensitive than the conventional method using hippuryl-histidyl-leucine (HHL) as a substrate. 2,3 However, in the proposed method, the use of an Fkit for the determination of 3-hydroxybutyrate (3HB) resulted in high cost and a long reaction time. In addition, the manipulation of the F-kit was inconvenient because of the smaller dispersion of reagents due to the high viscosity of a potassium phosphate/triethanolamine buffer solution containing an octylphenol ethylene oxide condensate (Triton X-100, used to solubilize proteins and improve the solubility of formazan) 4,5 when the assay reagents were mixed together.…”

Section: Introductionmentioning

confidence: 99%

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Assay of Angiotensin I-converting Enzyme-inhibiting Activity Based on the Detection of 3-Hydroxybutyrate with Water-soluble Tetrazolium Salt

et al. 2008

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A newly synthesized substrate, 3-hydroxybutyrylglycyl-glycyl-glycine (3HB-GGG), was applied to the assay of ACEinhibiting activity to overcome the smaller selectivity and sensitivity of the conventional method. In this study, an ACEinhibiting assay was improved by the use of a water-soluble tetrazolium salt, 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate sodium salt (WST-1), for the detection of 3-hydroxybutyrate, derived from 3HB-GGG. The optimized conditions were as follows: 0.333 mM NAD + , 0.333 mM WST-1, 0.1 mM EDTA, 0.633 U ml -1 diaphorase, and 0.700 U ml -1 3-hydroxybutyrate dehydrogenase. The developed assay was efficiently applicable to evaluate the ACEinhibiting activity of practical ACE inhibitors.

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Assay of angiotensin I-converting enzyme-inhibiting activity based on the detection of 3-hydroxybutyric acid

Cited by 27 publications

References 11 publications

Inhibition of Angiotensin-Converting Enzyme by Components of Traditional Mongolian Fermented Milk Products

Inhibition of Angiotensin-Converting Enzyme by Components of Traditional Mongolian Fermented Milk Products

Inhibition Activity of Angiotensin Converting Enzyme (ACE) and Determination of Total Phenolic and Flavonoid Compound from Bitter Melon Leaves (Momordica charantia L.)

Assay of Angiotensin I-converting Enzyme-inhibiting Activity Based on the Detection of 3-Hydroxybutyrate with Water-soluble Tetrazolium Salt

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