A rapid and simple spectrophotometric assay of angiotensin-converting enzyme

Hayakari, Makoto; Kondo, Yoshikazu; Izumi, Hiroshi

doi:10.1016/0003-2697(78)90053-2

Cited by 194 publications

(118 citation statements)

References 10 publications

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“…ACE was prepared according to Hayakari et al (1978) Rabbit lungs were used as starting material and the aliquots obtained were stored at -20°C for no more of two months. ACE inhibition from GS and IS aliquots, was evaluated in 20 µL of solution from these samples.…”

Section: Ace Inhibitory Activitymentioning

confidence: 99%

“…The resulting fractions were collected for assaying ACE inhibitory activity according to Hayakari et al (1978). Peptide molecular masses were determined by reference to a calibration curve created by running molecular mass markers on the Sephadex G-50 under conditions identical to those used for the test samples.…”

Section: G-50 Gel Filtration Chromatographymentioning

confidence: 99%

“…Elution was achieved by a linear gradient of acetonitrile in water (0-30% in 50 min) containing 0.1% trifluoroacetic acid at a flow rate of 4 mL/min and 30 °C [10]. Elution was monitored at 215 and 280 nm, and the resulting fractions were collected for assay of ACE inhibitory activity as described previously (Hayakari et al, 1978). The fractions with higher ACE inhibitory activity were injected in an analytical HPLC reverse phase column (C18 Hi-Pore RP-318, 250 mm × 4.6 mm BID-RAD column) for the analysis of ACE inhibitory activity in individual peaks.…”

Section: Hplc C18 Chromatographymentioning

confidence: 99%

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ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins

Magaña¹,

Campos²,

Dávila-Ortíz³

et al. 2015

Food Sci. Technol (Campinas)

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Phaseolus lunatus protein concentrates and the proteases Alcalase (R) and Pepsin-Pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Protein concentrate obtained from germinated and ungerminated seeds flour was hydrolyzed with Alcalase (R) at enzyme/substrate ratio (E/S) 1/10 and during 0.5 and 2.0 h, respectively. Dn the other hand, protein concentrate obtained from ungerminated (E/S: 1/10) and germinated (E/S: 1/50) seeds flour was sequentially hydrolyzed with Pepsin-Pancreatin during 1.0 and 3.0 h, respectively. Peptide fractions with ACE inhibitory activity in a range of 0.9 to 3.8 µg/mL were obtained by G-50 gel filtration chromatography and high-performance liquid chromatography C18 reverse phase chromatography. The observed amino acid composition suggests a substantial contribution of hydrophobic residues to the peptides' inhibitory potency, which potentially acts via blocking of angiotensin II production. These results show that P. lunatus seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with Alcalase (R) and Pepsin-Pancreatin.Keywords: P. lunatus; hydrolysates; peptides; ACE inhibitory activity.Practical Application: Legume proteins can enzymatically produce bioactive specific peptides for use in functional foods.

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Section: Ace Inhibitory Activitymentioning

confidence: 99%

Section: G-50 Gel Filtration Chromatographymentioning

confidence: 99%

Section: Hplc C18 Chromatographymentioning

confidence: 99%

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ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins

Magaña¹,

Campos²,

Dávila-Ortíz³

et al. 2015

Food Sci. Technol (Campinas)

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“…Inhibition of the renin angiotensin system ACE inhibition in vitro Enzyme activities were determined by Natoff et al (1985) using an assay based on the release of hippuric acid from the substrate Hip-His-Leu, originally described by Cushman & Cheung (1971) with the modification of Hayakari et al (1978). IC50 values were estimated from doseresponse curves (S -3 E + I) generated over a wide range of concentrations.…”

Section: Introductionmentioning

confidence: 99%

A review of the preclinical cardiovascular pharmacology of cilazapril, a new angiotensin converting enzyme inhibitor.

1989

Brit J Clinical Pharma

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1 Cilazapril is the monoethyl ester prodrug form of the di-acid cilazaprilat, a new angiotensin converting enzyme (ACE) inhibitor. Cilazaprilat has an IC50 of 1.9 nm as an inhibitor of rabbit lung ACE in vitro making it one of the most potent ACE inhibitors currently available. Studies on a wide range of other enzymes show that the inhibition is highly specific. 2 An oral dose of 0.1 mg kg-cilazapril evoked the same maximum degree of plasma ACE inhibition (-76%) in the rat as 0.25 mg kg-1 enalapril. Cilazapril (0.25 mg kg-' p.o.) inhibited plasma ACE by > 95%. The rate of recovery of ACE activity was slower with cilazapril (5-6% h-1) than with enalapril (10% h'-). 3 In anaesthetised rats cilazaprilat was equipotent with ramiprilat and slightly more potent (1.5 x) than enalaprilat as an inhibitor of the angiotensin I pressor response. 4 Following oral administration to conscious rats and intravenous administration to anaesthetised dogs, cilazapril was 2-4.5 x more potent than enalapril as an ACE inhibitor. 5 In cats cilazapril (0.1 and 0.3 mg kg-p.o.) dose dependently decreased plasma ACE activity and the angiotensin pressor response. Peak effects occurred at 2 h after dosing and plasma ACE inhibition was maintained at : 50% for up to 18 h. Mean arterial pressure was also decreased dose dependently with a peak effect at 3-4 h.6 Daily oral dosing of cilazapril (30 mg kg-1 p.o.) to spontaneously hypertensive rats evoked a progressive and prolonged (24 h) antihypertensive response with a maximum decrease in systolic blood pressure of 110 mm Hg. 7 Cilazapril (10 mg kg-1 p.o. twice daily for 3.5 days) progressively decreased blood pressure in volume depleted renal hypertensive dogs. The maximum fall in systolic pressure was 39 ± 6 mm Hg. 8 Haemodynamic studies in open chest anaesthetised dogs showed that the hypotensive response to intravenous cilazapril was accompanied by a reduction in total peripheral resistance. Small decreases in cardiac output and myocardial contractile force were seen at high doses. 9 Cilazapril had no adverse effect on cardiovascular reflexes. There was no impairment of the baroreflex in rats. Exercise-induced tachycardia and pressor responses in conscious cats were unchanged. 10 Cilazapril is exceptionally well absorbed by the oral route (98% in rats).

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“…HPLC is laborious and expensive, whereas the colorimetric assay is much more convenient. This assay was developed as a method for measurement of CPN (11) or angiotensin-converting enzyme (ACE) (8).…”

mentioning

confidence: 99%

Effect of Anticoagulants in Colorimetric Assay for Basic Carboxypeptidases

Komura

Obata

Campbell

et al. 2002

Microbiology and Immunology

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Carboxypeptidases (CP) in plasma and sera serve as regulators of anaphylatoxins such as C3a and C5a. The activity of CP can be measured by determining hippuric acid after cleavage of the small synthetic substrate hippuryl‐l‐arginine. Although a colorimetric assay is convenient for determining hippuric acid generated by CP, we noticed that some anticoagulants, such as citrate, interfere with the color development of the reagents used. EDTA and heparin provide an appropriate value. EGTA used as anticoagulant also provides an appropriate value. Therefore, concentration of citrate in samples should be controlled to be constant for background subtraction.

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A rapid and simple spectrophotometric assay of angiotensin-converting enzyme

Cited by 194 publications

References 10 publications

ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins

ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins

A review of the preclinical cardiovascular pharmacology of cilazapril, a new angiotensin converting enzyme inhibitor.

Effect of Anticoagulants in Colorimetric Assay for Basic Carboxypeptidases

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