• Title/Summary/Keyword: ACE 1

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Effect of N-Acetylcysteine on the Supetoxide Release, Chemotaxis from the Neutrophils and Glutathione Level of Plasma and Neutrophils (N-Acetylcysteine이 호중구의 Superoxide, Chemotaxis 및 혈장과 호중구의 Glutathione에 미치는 영향)

  • Song, Jeong-Sup;Lee, Sook-Young;Moon, Hwa-Sik;Park, Sung-Hak
    • Tuberculosis and Respiratory Diseases
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    • v.41 no.5
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    • pp.475-483
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    • 1994
  • Background: N-acetylcysteine(ACE) is used both orally and intravenously in a variety of experimental pathologies resembling human disease states which exhibit endothelial toxicity as a result of oxidative stress, including acute pulmonary oxygen toxicity, septicemia and endotoxin shock. Despite these observations in vivo, it is not certain how this thiol drug produces its protective effects. ACE is a cysteine derivative which is able to direct1y react with oxygen radicals and may also act as a cysteine and glutathione(GSH) precursor following deacetylation. In this paper, we tried to know whether the therapeutic doses of ACE can modify the inflammatory function of the neutrophils and can increase the glutathione level of plasma in chronic obstructive pulmonary disease(COPD) patients. In addition, the effect of ACE to the purified neutrophil in terms of superoxide release and glutathione synthesis were observed. Method: Firstly, we gave 600mg of ACE for seven days and compare the release of superoxide, luminol-enhanced chemiluminescence from the neutrophils, neutrophil chemotaxis, and plasma GSH levels before and after ACE treatment in COPD patients. Secondly, we observed the dose dependent effect of ACE to the purified neutrophil's superoxide release and GSH levels in vitro. Results: 1) Usual oral therapeutic doses(600mg per day) of ACE for seven days did affect neither on the neutrophil's superoxide release, chemiluminescence, chemotaxis, nor on the plasma GSH concentration in the COPD patients. 2) ACE decreases the purified neutrophil's superoxide release and increase the GSH production in dose dependent fashion in vitro. Conclusion: Despite the fact that oral ACE treatment did not affect on the neutrophil's inflammatory function and plasma GSH concentration in COPD patients in usual therapeutic doses, it decreases the superoxide release and increases the GSH production from the isolated neutrophils in high molar concentrations. These findings suggest that to obtain an antioxidative effects of ACE, it might be needed to increase the daily dosage of ACE or therapeutic duration or change the route of adminisration in COPD patients.

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Inhibitory Effect of Onion Seasoning on Angitensin Converting Enzyme (양파 조미액의 Angiotensin Converting Enzyme 저해활성)

  • 마상조
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.29 no.3
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    • pp.395-400
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    • 2000
  • 양파 조미액으로부터 ACE 저해활성 물질을 분리하기 위해 hexane, ethylether, ethylacetate, butanol과 물로 분획시, 4.8g의 당 함량과 31.9 mg의 phenol성 물질을 함유한 butanol 분획이 82.1%의 ACE 저해활성을 나타내었고, 70.3%의 ACE 저해활성을 보인 양퍄 조미액보다 높은 저해활성을 보였다. Butanol 분획을 Amberite XAD-2column으로 분리한 결과, ACE 저해활성을 보이는 미흡착 분획(F1)를 얻었다. 활성분획 F1을 Sephadex LH-20column으로 분획한 결과, 4개(F1-1,F1-2,F1-3,F1-4)의 분획을 얻었으며, 이중 F1-3 분획의 ACE 저해활성은 93%로 가장 높은 저해활성을 보였다. Sephadex LH-20 column chromatography에 의해 얻어진 활성분획F1-3을 Supercosil LC-18 column을 이용하여 분리한 결과, 6분대에서 ACE 저해활성을 가지는 단일 peak(F1-3a)를 얻었다. 각 정제 과정에서 얻은 분획들은 전형적인 flavonoid의 band I과 bandII의 피크를 보였다. 또한 ACE에 대한 저해기작은 flavonoid 물질이 보이는 전형적인 비경쟁적 저해양상을 보였다.

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Optimization of Skim Milk Fermentation Conditions by Response Surface Methodology to Improve ACE Inhibitory Activity Using Lactiplantibacillus plantarum K79 (반응표면법에 의한 Lactiplantibacillus plantarumK79를 이용한 ACE(Angiotensin Converting Enzyme) 억제활성 향상을 위한 탈지유 발효조건 최적화)

  • Park, Yu-Kyoung;Hong, Sang-Pil;Lim, Sang-Dong
    • Journal of Dairy Science and Biotechnology
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    • v.40 no.3
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    • pp.93-102
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    • 2022
  • This study was conducted using response surface methodology (RSM) to elucidate fermentation conditions that will optimize ACE inhibitory activity using Lactiplantibacillus plantarum K79. Four independent variables [skim milk (with 1% added glucose) concentration (6%-14%), incubation temperature (32℃-42℃), incubation time (8-24 h), and amount of added starter (0.02%-0.2%)] were evaluated using five-level central composite design and response surface methodology to determine the optimum fermentation condition. The dependent variables were angiotensin converting enzyme (ACE) inhibitory activity (the value obtained from 102 diluted supernatant), and pH. The respective coefficients of determinations (R2) were 0.791 and 0.905 for ACE inhibitory activity and pH. The maximum ACE inhibitory activity was 90% under the following conditions: 10% skim milk (with 1% added glucose) concentration, 37℃ incubation temperature, 17.8 h incubation time, and 0.2% added starter. Based on the RSM, using predicted best ACE conditions for fermentation of 13.49% skim milk (with 1% added glucose) with 0.0578% starter at 33.4℃ for 21.5 h, the predicted ACE inhibitory activity and pH values were 86.69% and 4.6, respectively. Actual ACE inhibitory activity and pH values were 85.5% and 4.58, respectively

Effects of Angelicae Pubescentis Radix Water Extract on Immune Property in RAW 264.7 Macrophages (독활 물 추출물이 대식세포 면역 활성에 미치는 영향)

  • Lee, Jong-Han;Kim, Yoon-Sang;Lim, Eun-Mee
    • The Journal of Korean Medicine
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    • v.32 no.1
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    • pp.175-184
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    • 2011
  • Objectives: The purpose of this study was to investigate the effects of Angelicae pubescentis Radix water extract (ACE) on immune properties in macrophage cells. Methods: The cells were divided into two groups: As a control, the first was not treated with ACE, and the other was treated with ACE. Together with the cell viability, productions of nitric oxide (NO) and cytokines such as interleukin (IL)-$1{\beta}$, IL-6, and tumor necrosis factor (TNF)-${\alpha}$ by treating of ACE were monitored. Results: 1. There was no decrease of the cell viability after 24 hr incubation, but a significant decrease after 48 hr incubation with all four concentrations (25, 100, 200, and $400\;{\mu}g/m{\ell}$) of ACE. 2. A significant increase in the production of NO was observed in the concentrations above $50\;{\mu}g/m{\ell}$ of ACE after 24 hr incubation. 3. Further, after 48 hr incubation, the critical concentration of ACE for the increase was reduced to $25\;{\mu}g/m{\ell}$. 4. The production of (IL)-$1{\beta}$ significantly increased with the ACE concentrations of 100 and $200\;{\mu}g/m{\ell}$ after 24 hr incubation. 5. The production of IL-6 significantly increased with the ACE concentration of $200\;{\mu}g/m{\ell}$ after 24 hr incubation. 6. A significant increase in the production of (TNF)-${\alpha}$ was detected with ACE concentrations of 50, 100, and $200\;{\mu}g/m{\ell}$ after 24 hr incubation. Conclusions: These show that ACE increases mouse macrophage NO production at concentrations above $50\;{\mu}g/m{\ell}$, and the cytokines ((IL)-$1{\beta}$, IL-6, and (TNF)-${\alpha}$) at concentrations above $200\;{\mu}g/m{\ell}$. These results suggest that ACE improves macrophage immune property.

Evaluation of Angiotensin -I- Converting Enzyme Inhibitory Activity and Protein Changes of Enzymatic Hydrolysate Extracted from Hanwoo Loin and Round Myosin B (한우 등심과 우둔에서 추출한 Myosin B의 효소적 가수분해물의 단백질 변화와 Angiotensin -I- Converting Enzyme(ACE) 저해효과)

  • Kim, Y.J.;Chin, Koo-Bok
    • Journal of Animal Science and Technology
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    • v.49 no.1
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    • pp.129-136
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    • 2007
  • This study was performed to determine the protein profiles using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Angiotensin-I-converting enzyme(ACE) inhibitory activity (IC50) as affected by the various meat cuts, digestion times with pepsin. Hydrolysates having the protein concentration of 10 ug/mL had approximately 36∼39% ACE inhibitory activities, regardless of meat cut and digestion time. Protein concentration and ACE inhibitory activity of the diluted hydrolysate increased after 1-hr digestion. In original hydrolysates, ACE inhibitory activities of loin had higher than those of round (P<0.05). In addition, non-heated hydrolysates had higher ACE inhibitory activities than heated counterparts. When myosin B was digested by pepsin more than 1 hr, improved ACE inhibitory activities were observed as compared to the non-digested control.

OCC 고지의 원료 특성 연구

  • 조신환;이종필;구재은;김현호
    • Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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    • 2000.11a
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    • pp.131-131
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    • 2000
  • 백판지, KL, 지관원지, 석고원지 등의 산업 용지 지종에 주로 ace 계통의 저급 고지가 원료 로 주로 사용되고 있다 .. ace 고지는 크게 원산지별로 약간씩 상이한 물성을 나타내고 있는데 각 원지 요구 특성도 각각 다양하다. 효율적인 ace 고지의 이용을 위해서는 ace 고지 자체의 외관 특성 및 물리적인 특성을 정확하게 파악하는 것이 중요하다. 그러므로 본 연구에서는 각 O ace 원료의 특성을 파악하여 각 원지 특성에 적합한 물성을 나타내기 위한 ace data를 얻고 자하였다. 미산 ace, 국산 ace, 일본 ace의 물성을 측정하였다. 실험 결과 열단장이 각각 2.94, 2. 3 35, 2,2km로 미산 ace가 가장 우수하였고, 국산과 일본 ace 는 비슷한 열단장을 나타내고 있다. 파열강도도 역시 미산 ace가 가장 우수하였고, 국산과 일본 ace 는 비슷한 강도를 나 타내고 있다. 내절도의 경우에도(1.0kgf 압력하) 미산, 국산과 일본산이 각각 124, 19, 18회 를 나타내고 있다. 해리성의 경우에는 국산과 일본산은 98.9%의 해리율로 유사한 특성을 나타내고 있으나, 미 국산의 경우에는 89.0-96.9%로 상당히 낮은 해리율을 나타내고 있는데 미국산 ace의 경우에 는 습윤시 강도 향상을 위하여 습윤지력중강제의 투입으로 인하여 섬유 해섬에 방해가 되기 때 문이다. 해리성 향상을 위하여 펄핑 방법, 시간, 약품 (가성소다, 해리촉진제 등), Kneader 처 리 둥을 시도하여 보았다. 펄핑 시간과 가성소다의 투입 영향이 가장 큰 효과를 나타내었다. 이물질함량은 국산 ace가 가장 많았고, 미산, 일본산 ace가 가장 적었다.

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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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Yeast copper-dependent transcription factor ACE1 enhanced copper stress tolerance in Arabidopsis

  • Xu, Jing;Tian, Yong-Sheng;Peng, Ri-He;Xiong, Ai-Sheng;Zhu, Bo;Jin, Xiao-Fen;Gao, Jian-Jie;Hou, Xi-Lin;Yao, Quan-Hong
    • BMB Reports
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    • v.42 no.11
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    • pp.752-757
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    • 2009
  • Copper is essential but toxic in excess for aerobic organisms. Yeast transcription factor ACE1 functions as a sensor for copper and an inducer for the transcription of CUP1. In addition, ACE1 can activate the transcription of superoxide dismutase gene (sod1) in response to copper. In this study, we introduced the yeast ACE1 into Arabidopsis and analyzed its function in plant. Under high copper stress, the transgenic plants over-expressing ACE1 showed higher survival rate than the wild-type. We also found that over-expression of ACE1 in Arabidopsis increased the activities of SOD and POD, which were beneficial to the cell in copper buffering. Excess copper would suppress the expression of chlorophyll biosynthetic genes in Arabidopsis, RT-PCR analysis revealed that over-expression of ACE1 decrease the suppression. Together, our results indicate that ACE1 may play an important role in response to copper stress in Arabidopsis.

The Changes of Serum Angiotensin Converting Enzyme Activity in Lung Cancer Patients (폐암 환자의 혈청 Angiotensin Converting Enzyme 활성도의 변화)

  • Jeong, Ki-Ho;Choi, Hyung-Seok;Yoo, Chul-Gyu;Lee, Kye-Young;Kim, Young-Whan;Han, Sung-Koo;Shim, Young-Soo;Kim, Keun-Youl;Han, Yong-Chol
    • Tuberculosis and Respiratory Diseases
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    • v.39 no.4
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    • pp.310-317
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    • 1992
  • Background: Angiotensin converting enzyme is a glycoprotein peptidyldipeptide hydrolase which cleaves the c-terminal dipeptides of several oligopeptides. It is a menbrane-bound protein mainly synthesized by the endothelial cells. Since the lung has the largest capillary bed of any organ in the body, it is here that ACE acts on circulating substrates like angiotensin I and bradykinin. It is well known that ACE correlates with disease activity in sarcoidosis and also there are reports that changes in serum ACE activity are found in many acute and chronic lung diseases. So we planned this study to see if serum ACE activity can act as a prognostic factor in lung cancer. Methods: Forty-one newly diagnosed lung cancer patients were included in the study group. There were 19 patients with squamous cell lung cancer, 13 with adenocarcinoma, and 9 with small cell carcinoma. Patients were excluded from the study if they had high blood pressure, heart disease, liver disease, renal disease, or other lung disease. Serum ACE activity was analyzed according to cell type, staging, mode of treatment, and clinical response to treatment. Results: 1) There was no difference in serum ACE activity between lung cancer patients and the control group. Also no difference in serum ACE activity was found according to cancer cell type or staging. 2) In patients who underwent curative resection of lung cancer, serum ACE activity was decreased significantly after the operation. 3) In patients who were diagnosed as non-small cell lung cancer and were treated with 4 cycles of anti-cancer chemotherapy without clinical improvement, changes in serum ACE activity were not seen after the treatment. 4) In patients diagnosed as small cell lung cancer treated with 4 cycles of anti-cancer chemotherapy with clinical improvement, changes in serum ACE activity were also not observed. Conclusion: Serum ACE activity was decreased after lung resection but had no relation to cell type, staging, or clinical response to treatment in lung cancer patients. Therefore, serum ACE activity is not suitable in predicting clinical outcome of lung cancer patients.

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CoMFA and CoMSIA Study on Angiotensin-Converting Enzyme (ACE) Inhibitors: a Molecular Design of Potential Hypertensive Drugs

  • San Juan, Amor A.;Cho, Seung-Joo
    • Proceedings of the Korean Society for Bioinformatics Conference
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    • 2005.09a
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    • pp.249-255
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    • 2005
  • Angiotensin-converting enzyme (ACE) is primarily responsible for human hypertension. Current ACE drugs show serious cough and angiodema health problems due to the un-specific activity of the drug to ACE protein. The availability of ACE crystal structure (1UZF) provided the plausible biological orientation of inhibitors to ACE active site (C-domain). Three-dimensional quantitative structure-activity relationship (3D-QSAR) models have been constructed using the comparative molecula. field analysis (CoMFA) and comparative molecular similarity indices analysis (CoMSIA) for a series of 28 ACE inhibitors. Alignment for CoMFA obtained by docking ligands to 1UZF protein using FlexX program showed better statistical model as compared to superposition of corresponding atoms. The statistical parameters indicate reasonable models for both CoMFA (q$^2$ = 0.530, r$^2$ = 0.998) and CoMSIA (q$^2$= 0.518, r$^2$ = 0.990). The 3D-QSAR analyses provide valuable information for the design of ACE inhibitors with potent activity towards C-domain of ACE. The group substitutions involving the phenyl ring and carbon chain at the propionyl and sulfonyl moieties of captopril are essential for specific activity to ACE.

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