• Title/Summary/Keyword: Angiotensin-converting enzyme

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Inhibition Effect of Against Angiotensin Converting Enzyme of Flavan-3-ols isolated Korean Green Tea (한국산 녹차로부터 분리한 Flavan-3-ol 화합물의 Angiotensin Converting Enzyme 저해 효과)

  • Cho, Young-Je;An, Bong-Jeun;Choi, Cheong
    • Korean Journal of Food Science and Technology
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    • v.25 no.3
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    • pp.238-242
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    • 1993
  • For the Purpose of utilizing tannins in the functional foods and crude drugs, the enzyme inhibition of tannins isolated from Korean green tea were determined. Acetone extract from Korean green tea showed inhibition effect against the angiotensin converting enzyme. The galloyl tannins showed higher inhibition activity against angioteosin converting enzyme than the nongalloyl tannins. In terms of stereo isomers, (-)-epicatechins had higher inhibition activity than the (+ )-catechins. The synergistic activity was also observed. Tannins isolated from Korean green tea appeared to be incompetitive inhibitor against the angiotensin converting enzyme.

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Analysis of the Components of Guibitang and Fermented Guibi-tang and their Ability to Inhibit Angiotensin-converting Enzyme

  • Liang, Chun;Yun, Na-Young;Jung, Sang-Won;Kim, Dong-Seon;Lee, Young-Jae;Ma, Jin-Yeul
    • Natural Product Sciences
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    • v.17 no.4
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    • pp.363-366
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    • 2011
  • Guibi-tang is a traditional medicine used for the treatment of colds. We investigated the levels of several compounds in Guibi-tang before and after fermentation with Lactobacillus and tested their ability to inhibit angiotensin-converting enzyme. Six known compounds (decursin, decursinol angelate, nodakenin, liquiritin, formononetin, and 6-gingerol) and 2 unidentified compounds were detected in Guibi-tang (GB) and fermented Guibi-tang (FGB) by an established HPLC-DAD method. The levels of the 6 known compounds were decreased after fermentation. FGB showed more potent inhibition of angiotensin-converting enzyme activity than GB. In conclusion, fermentation with Lactobacillus affects the content of several compounds in GB and improves its angiotensin-converting enzyme inhibitory activity.

Isolation of Angiotensin I Converting Enzyme (ACE) Inhibitor from fermented oyster, Crassostrea gigas

  • Park, Ji-Young;Je, Jae-Young;Park, Pyo-Jam;Kim, Se-Kwon
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2002.10a
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    • pp.193-194
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    • 2002
  • Angiotensin I converting enzyme (ACE) inhibitor was purified from Crassostrea gigas. The ACE belongs to the class of metalloprotease. This enzyme plays an important physiological role in regulating blood pressure of the rennin-angiotensin system by converting from angiotensin I to octapeptide angiotensin II, a potent vasoconstrictor and by inactivating bradykinin, which has depressor action. (omitted)

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Production of Angiotensin I Converting Enzyme Inhibitory Peptides from Bovine Blood Plasma Proteins (도축 폐혈액 단백질로부터의 Angiotensin I Converting Enzyme 저해 펩타이드의 생산)

  • Hyeon, Chang-Gi;Sin, Hyeon-Gil
    • KSBB Journal
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    • v.14 no.5
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    • pp.600-605
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    • 1999
  • For the production of angiotensin I converting enzyme inhibitory peptides as a material for antihypertensive functional foods from animal blood produced in slaughterhouse, the optimum condition for enzymatic hydrolysis to yield a peptide fraction of the highest activity were investigated with a respect of industrial production. Among several industrially-usable enzymes tested, $Alcalase^?$ produced hydrolysates of the highest activity from total plasma and purified albumin. $IC_50$ values of albumin hydrolysate and its third fraction separated by gel chromatography were 0.5 and 0.02 mg/mL, respectively. The fraction was found to be obtained by a simple ultrafiltration using a membrane of MW cutoff 1,000. The possibility for the industrial production of antihypertensive peptides from animal blood plasma protein was suggested.

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Isolation of Angiotensin Converting Enzyme Inhibitory Peptide from Beef Bone Extract Hydrolysate

  • Park, Eun-Hee;Cho, Yong-Sik;Song, Kyung-Bin
    • Applied Biological Chemistry
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    • v.41 no.4
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    • pp.270-272
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    • 1998
  • Angiotensin converting enzyme (ACE) inhibitor was isolated from beef bone extract hydrolysate. After hydrolysis of beef bone extract with a commercial protease, ACE inhibitory peptide was purified by using ultrafiltration, gel permeation chromatography, and reverse-phase high pressure liquid chromatography. The purified ACE inhibitor was a pentapeptide, Gly-Pro-X-Gly-Pro.

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구기자(Lycium chinence Miller) 첨가 요구르트의 항산화 활성과 ACE 저해 및 ${\alpha}-glucosidase$ 저해 효과

  • Bae, Hyeong-Cheol;Jo, Im-Sik;Nam, Myeong-Su
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • 2005.05a
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    • pp.326-330
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    • 2005
  • 구기자, 구기엽, 지골피 추출물을 이용한 요구르트를 제조하여 항산화효과, ACE (angiotensin converting enzyme) 저해 효과 및 ${\alpha}-glucosidase$ 저해 활성을 시험하였다. 구기자 첨가 발효유의 Antioxidants activity는 물 추출물보다 methanol 추출물에서 더 많은 항산화 활성능을 보였으며 특히 구기엽 요구르트에서 83.85%의 높은 활성능을 보였다. 구기자와 지골피 요구르트에서는 각각 47%와 54%내외의 활성능을 나타냈다. 구기자 첨가 발효유의 ACE(angiotensin converting enzyme) 저해 효과는 원재료에서는 물 추출물이 angiotensin converting enzyme 저해능이 높았고, 구기자 요구르트의 경우 물 추출물과 methanol 추출물 모두가 angiotensin converting enzyme 저해능이 높은 것으로 나타났다. 구기자 첨가 발효유의 ${\alpha}-glucosidase$ 저해 활성은 구기자, 구기엽 및 지골피 4% 첨가 요구르트에서 methanol 추출물의 경우 각각 8.2%, 5.6%, 7.3%의 ${\alpha}-glucosidase$ 저해능을 나타냈는데 이들 모두 원재료 보다는 활성 저해능이 큰 것으로 나타났으나 물 추출물의 경우에는 활성 저해능이 거의 나타나지 않았다.

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Properties of Angiotensin I-Converting Enzyme Activity in the Rice Eel, Monoptevus albus (드렁허리(Monopterus albus)의 Angiotensin I-Converting Enzyme의 특성에 관하여)

  • 김성주;이금영;조경우
    • The Korean Journal of Zoology
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    • v.34 no.2
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    • pp.142-147
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    • 1991
  • Angiotensin I-converting enzyme (ACE) activity has been characterized in the rice eel, Monopterus albus. Peak activity of ACE in plasma from the rice eel was shown at around pH 10, which was more alkaline compared to that of mammals. Chloride requirements for the optimal ACE activity were different from species to spedes. ACE inhibitors, EDTA, teprotide (SQ 20, 881), and captopril (SQ 14, 225) showed dose-dependent inhibitions of ACE activity in plasma from the rice eel as well as mammals. ACE activity in the rice eel was increased by CoCI2, and the enzyme activity was more unstable at high temperature as compared to mammals The highest activity of ACE among the various tissues in the rice eel was found in the brain.

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A Case of Angioedema Induced by Angiotensin-Converting Enzyme Inhibitor (Angiotensin-Converting Enzyme Inhibitor(ACE Inhibitor)에 의해 유발된 안면부 맥관부종(angioedema) 치험례)

  • Hsia, Yu-Chun;Jung, Ki-Yong;Baik, Jong-Woo;Kim, Dong-Woo;Park, Jong-Hyung;Jun, Chan-Yong;Choi, You-Kyung
    • The Journal of Internal Korean Medicine
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    • v.28 no.2
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    • pp.399-407
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    • 2007
  • Angioedema is a localized transient swelling of sudden onset that can occur in the face, lips, tongue, hand, feet, respiratory system and gastrointestinal system. Angioedema is classified as allergy, hereditary, idiopathic or induced by medication as like aspirin, nonsteroidal anti-inflammatory agents, opiates, antibiotics, and angiotensin-converting enzyme. Angiotensin-converting enzyme inhibitors are widely prescribed for hypertension and heart failure. This drug is commonly associated with angioedema which may be potentially life threatening. We experienced a case of angioedema induced by ACE inhibitor (angiotensin-converting enzyme inhibitor) in a 74-year-old patient who took ACE inhibitor to control hypertension during hospitalization. We thought the angioedema in the face had relation to myenzhong (面腫, mienjong) in oriental medicine. Weiling-tang (Wiryung-tang) was effective for angioedema in the face. As a result the symptoms disappeared rapidly. After 6 days, the patient's symptoms had notably improved.

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Angiotensin Converting Enzyme Inhibitory Activity of BR-900317 in vivo, and Antihypertensive Effect of its Single Oral Administration on Blood Pressure and Effect on the Renin-angiotensin System in Hypertensive Model Rats (SHR, RHR) (BR-900317의 In vivo에 있어서 Angiotensin 변환효소 저해작용 밀 고혈압 model rat (SHR, RHR)에 있어 단회 경구투여에 의한 강압작용)

  • 장경진;김지한;백우현
    • Biomolecules & Therapeutics
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    • v.1 no.2
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    • pp.220-225
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    • 1993
  • Effect of BR-900317 on the angiotensin I-induced pressor response in pithed rats and the effects of its single oral administration on plasma angiotensin converting enzyme (ACE) activities in normotensive rats and on the cardiovascular system in hypertensive model rats (SHR, RHR), were compared with those of captopril. BR-900317 attenuated the angiotensin I-induced pressor effects in pithed rats. In a single oral dose administration study, BR-900317 inhibited the plasma ACE activities in a dose-dependent fashion. Duration of the action of BR-900317 was similar to that of captopril. BR-900317 produced antihypertensive effect in spontaneously hypertensive rats and dose-dependent antihypertensive effect in 2-kidney Goldblatt hypertensive rats without affecting heart rate. These results suggest that the main mechanism of the antihypertensive effect of BR-900317 is the suppression of angiotensin II production due to the inhibition of the ACE.

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Analysis of Angiotensin I Converting Enzyme Inhibitory Activity of Oligosacchride Extracted from Capsosiphon fulvescens (매생이 유래 올리고당의 추출 분리 및 Angiotensin I Converting Enzyme 저해능 분석)

  • Kim, Hyun-Woo;Lee, Jung-Heon
    • KSBB Journal
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    • v.28 no.2
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    • pp.131-136
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    • 2013
  • The hydrolysates prepared with various enzyme digestion of Capsosiphon fulvescens were used to measure the inhibitory effects against angiotensin I converting enzyme (ACE). The commercially available enzymes such as Celluclast, Viscozyme, Lysing enzyme, Flavourzyme, Alcalase and Pectinex were used to digest C. fulvescens and produce hydrolysates. The maximum ACE inhibitory activity was observed using Alcalase hydrolysis (72.9%). The optimal conditions of Alcalase extraction were pH 8.0 and extraction time for 12 hr. The hydrolysates were fractionated using preparative-LC and anion-exchange chromatography on DEAE-cellulose and the fraction B and B-2 were isolated. The ACE inhibitory activity of fraction B-2 by anion-exchange chromatography was 82.6%. The molecular weight of fraction B-2 estimated using size exclusion chromatography was about 1 kDa. The monosaccharide composition of the fraction B-2 was determined to be mannose (1.1%), glucuronic acid (1.3%), galactose (1.3%) and glucose (96.3%).