• Title, Summary, Keyword: angiotensin-converting enzyme

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Screening of Plant Materials for the Inhibitory Activities Against Angiotensin Converting Enzyme (식물생약(植物生藥)의 안지오텐신변환효소(變換酵素) 억제작용(抑制作用) 검색(檢索))

  • YunChoi, Hye-Sook;Chung, Sung-Hyun;Han, Byung-Hoon
    • Korean Journal of Pharmacognosy
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    • v.12 no.1
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    • pp.51-54
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    • 1981
  • Twenty-seven medicinal plants were selected on the basis of folkloric reputation for the treatment of hypertension or related deseases. Two solvent fractions were prepared from methanol extract of each plant and tested for their effects on angiotensin converting enzyme (ACE) activities. Six solvent fractions showed more than 50% inhibition and four showed $40{\sim}50%$ inhibition at the conditions tested.

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Epoxyalkanoyls as Novel ACE Inhibitors

  • P. Choo, Hea-Young;Yoon, Hea-Ran;Park, Hwha-Soon;Kim, Dong-Hyun;Park, Jong-Sei;Kim, Dong-H.
    • Archives of Pharmacal Research
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    • v.21 no.2
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    • pp.168-173
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    • 1998
  • The epoxyalkanoyl derivatives were designed and synthesized as ACE inhibitors. Coupling of unsaturated carboxylic acids with amino acids and following epoxidation with dimethyldioxirane gave the epoxyalkanoyls with high yield. The inhibitory activity of synthesized compounds on angiotensin converting enzyme was $IC_{50}$ values of 0.06~5.5 ${\mu}M$.

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Production of Angiotensin-I Converting Enzyme Inhibitory Hydrolysates from Egg Albumen

  • Kim, H.S.;Ham, J.S.;Jeong, S.G.;Yoo, Y.M.;Chae, H.S.;Ahn, C.N.;Lee, J.M.
    • Asian-Australasian Journal of Animal Sciences
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    • v.16 no.9
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    • pp.1369-1373
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    • 2003
  • ACE (Angiotensin-I converting enzyme) inhibitory peptides derived from foods are thought to suppress high blood pressure by inhibiting ACE. We tried to make efficient production of the ACE inhibitory hydrolysate from egg albumen. A hydrolysate digested by neutrase presented the highest ACE inhibitory activity ($IC_50\;value=256.35{\mu}g/ml$) and the proper proteolysis was occurred by 1.0% enzyme addition and 4 h incubation at $47^{\circ}C$. Antihypertensive effect of neutrase hydrolysate was investigated in spontaneously hypertensive rats (SHR, n=5). Systolic blood pressure (SBP) was decrease by 6.88% (-14.14 mmHg, p<0.05) at 3 h after oral administration of 300 mg/kg body weight, and by 13.33% (-27.72 mmHg, p<0.05) by emulsified hydrolysate. These results showed that it is very effective to utilize egg albumen as a protein source for the production of ACE inhibitory peptides. However, further studies are required to investigate the methods to increase recovery yield and the isolation of active peptide is necessary for determining its sequence responsible for ACE inhibitory activity.

Abalone Protein Hydrolysates: Preparation, Angiotensin I Converting Enzyme Inhibition and Cellular Antioxidant Activity

  • Park, Soo Yeon;Je, Jae-Young;Hwang, Joung-Youl;Ahn, Chang-Bum
    • Preventive Nutrition and Food Science
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    • v.20 no.3
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    • pp.176-182
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    • 2015
  • Abalone protein was hydrolyzed by enzymatic hydrolysis and the optimal enzyme/substrate (E/S) ratios were determined. Abalone protein hydrolysates (APH) produced by Protamex at E/S ratio of 1:100 showed angiotensin I converting enzyme inhibitory activity with $IC_{50}$ of 0.46 mg/mL, and APH obtained by Flavourzyme at E/S ratio of 1:100 possessed the oxygen radical absorbance capacity value of $457.6{\mu}M$ trolox equivalent/mg sample. Flavourzyme abalone protein hydrolysates (FAPH) also exhibited $H_2O_2$ scavenging activity with $IC_{50}$ of 0.48 mg/mL and $Fe^{2+}$+ chelating activity with $IC_{50}$ of 2.26 mg/mL as well as high reducing power. FAPH significantly (P<0.05) protected $H_2O_2$-induced hepatic cell damage in cultured hepatocytes, and the cell viability was restored to 90.27% in the presence of FAPH. FAPH exhibited 46.20% intracellular ROS scavenging activity and 57.89% lipid peroxidation inhibition activity in cultured hepatocytes. Overall, APH may be useful as an ingredient for functional foods.

Peptide Inhibitors for Angiotensin I Converting Enzyme from Corn Gluten Digests. (옥수수 글루텐 효소 가수분해물의 Angiotensin I Converting Enzyme 활성 저해 펩타이드의 정제)

  • 오광석;이동건;홍정운;성하진
    • Microbiology and Biotechnology Letters
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    • v.31 no.1
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    • pp.51-56
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    • 2003
  • The angiotensin I converting enzyme (ACE) has an important role in the maintenance of blood pressure. The ACE inhibitory activities of foods have recently been studied. We tried to isolate ACE inhibitory peptides from the Flavourzyme (FZ), Pescalase (PE), and Thermolysine (TH) protease digests of corn gluten, which was restricted to the use the source of food for digestion problem. The FZ, PE, TH/PE protease hydrolyzed corn gluten and the inhibitory activities of the hydrolyzates for ACE were measured. Major fractions were isolated from the digests using ODS chromatography after treating with ethanol in step gradient. The ACE inhibitors were further purified by Bio-Gel P-2 column and reverse phase HPLC. Five inhibitory peptides were isolated. Their amino acids were sequenced as LPF ($IC_{50}$ = 40$\mu$M), GPP ($IC_{50}$ = 17.6$\mu$M), PNPY ($IC_{50}$ = 30.7$\mu$M), SPPPFYL ($IC_{50}$ = 63 $\mu$M), and SQPP ($IC_{50}$ = 17.2$\mu$M).

Characteristics of Angiotensin Converting Enzyme Inhibitory Peptides from Thermolysin Hydrolysate of Manila clam, Ruditapes philippinarum Proteins (바지락 단백질 Thermolysin 가수분해물의 Angiotensin Converting Enzyme 저해 Peptide의 특성)

  • Lee Tae Gee;Yeum Dong Min;Kim Seon Bong
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.35 no.5
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    • pp.529-533
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    • 2002
  • The peptides inhibiting angiotensin converting enzyme (ACE) were isolated from the hydrolysate of manila clam (Ruditapes philippinamm) proteins prepared with thermolysin. The thermolysin hydrolysate was pretreated with membrane filter (MW cut-off 10,000) to obtain the peptide fraction with ACE inhibition. The crude peptides were applied to a Sephadex LH-20 column and eluted with $30\%$ methanol. The three active fractions (A, B and C) were collected and concentrated, and then applied to a SP-Toyopearl 650S column equilibrated with distilled water and was eluted with a linear gradient of NaCl concentration (0 to 1 M). The four active fractions (A-1, A-2, B-1 and C-1) were collected and concentrated, and then applied to a SuperQ-Toyopearl 650S column equilibrated with distilled water and was eluted with a linear gradient of NaCl concentration (0 to 1 M). The maximum inhibitory activity was observed in the fraction B-1Q showed the IC_{50} values of 0.748 $\mu$g. The abundant amino acids obtained from active fraction B-1Q were leucine, isoleucine, alanine and threonine.

Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Recombinant E. coli (재조합 대장균으로부터 항고혈압 Angiotensin I-Converting Enzyme 저해제의 특성연구)

  • Kim, Jae-Ho;Jeong, Seung-Chan;Lee, Dae-Hyong;Lee, Jong-Soo
    • The Journal of Natural Sciences
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    • v.16 no.1
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    • pp.1-13
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    • 2005
  • The angiotensin I-converting enzyme (ACE) inhibitor has anti-hypertensive effects and has long been used as prevention or remedy of hypertension. This study were carried out to produce and purify a new ACE inhibitor from recombinant E. coli and further elucidate its structure-function relationship. Recombinant pGEX-4T-3 containing ACE inhibitory peptide gene of Saccharomyces cerevisiae was transformed into E. coli BL21(DE3). Glutathione-S transferase (GST) fusion protein from E. Coli BL21(DE3) harboring the recombination pGEX-4T-3 was obtained and the ACE inhibitory peptide was purified with Sephadex G-25 column chromatography. The purified ACE inhibitory peptide was a novel decapeptide with sequence Tyr-Asp-Gly-Gly-Val-Phe -Arg-Val-Tyr-Thr which shows very low similarity to the other ACE inhibitory peptide sequence. The purified ACE inhibitor competitively inhibited ACE.

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Characteristics of Angiotensin Converting Enzyme Inhibitory Peptides from Salt-fermented Squid Liver Sauce (오징어 간 액젓으로부터 분리된 Angiotensin Converting Enzyme 저해 Peptide의 특성)

  • Park, Yeung-Beom
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.39 no.11
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    • pp.1654-1659
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    • 2010
  • In order to utilize squid liver by-products, which is normally discarded as industrial waste in the process of squid manufacturing, salt-fermented squid liver sauce was prepared experimentally and also tested for inhibitory activity against angiotensin converting enzyme (ACE). ACE inhibitory activity of squid liver sauce was increased with the elapse of fermentation days until 12 months, followed by a constant level of inhibitory activity thereafter. 15-month-old sauce ($IC_{50}=29.66\;{\mu}g$) was filtered through PM-10 membrane (M.W. cut-off 10,000 Da) to obtain the peptides fractions with ACE inhibition activity. Filtered fractions were applied to a Bio-gel P-2 column and three active fractions (A, B and C) were collected. Among them, fraction B applied to a SuperQ-Toyopearl 650S column chromatography lead to the isolation of active B-1 fraction. It has the ACE inhibitory activity ($IC_{50}=5.46\;{\mu}g$). The main composition of its amino acids is lysine, glycine and proline, which cover about 85% of the total amino acids.

Isolation of Angiotensin Converting Enzyme Inhibitor from Doenjang (전통된장으로부터 Angiotensin Converting Enzyme 저해물질의 분리)

  • Kim, Seung-Ho;Lee, Yun-Jin;Kwon, Dae-Young
    • Korean Journal of Food Science and Technology
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    • v.31 no.3
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    • pp.848-854
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    • 1999
  • Inhibitory compounds of angiotensin converting enzyme (ACE) were separated from Doenjang (traditional Korean fermented soybean paste). Water extracts from Doenjang which showed ACE inhibitory activity were separated with gel permeation chromatography (GPC), in which two fractions with high ACE inhibitory activities were obtained. The first fraction from GPC was further isolated by semi-preparative reverse phase preparative-HPLC (high performance liquid chromatography) and 2-dimensional electrophoresis/thin layer chromatography (TLC). The purified spot had molecular weight of 759 daltons and ninhydrin-positive non-peptide. The second fraction from GPC was also further isolated by semi-preparative reverse phase HPLC and $NH_2-column$ HPLC. One fraction with high ACE inhibitory activity was purified and characterized. Molecular weight of this fraction by LC-MS was 272.34 daltons. The active fraction was identified as Arg-Pro with ACE $IC_{50}$ of $92\;{\mu}M$.

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The Clinical Study on Angiotensin Converting Enzyme Gene Polymorphism in Korean Facial nerve palsy Patients (한국인(韓國人) 구안와사(口眼喎斜) 환자(患者)의 Angiotensin Converting Enzyme 유전자(遺傳子) 다형성(多形成)에 관(關)한 임상연구(臨床硏究))

  • Hong, Jang-mu;Park, Dong-suk;Koh, Hyung-kyun
    • Journal of Acupuncture Research
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    • v.21 no.2
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    • pp.103-113
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    • 2004
  • Objective : This study was designed to investigate the relation between the angiotensin converting enzyme(ACE) gene polymorphism and Facial nerve palsy in the Korean population. Methods : This sudy was carried out on 117 Facial nerve palsy patients who were treated in the department of acupuncture & moxibustion, Hospital of Oriental medical college, Kyung-Hee University and 135 healthy control subjects. Blood samples from all subjects were obtaind for DNA extraction. The extracted DNA was amplified by polymerase chain reaction(PCR). PCR products were visualized by 2% agarose gel electrophoresis. Results : The sub-genotypes of ACE gene were II homozygotes, ID heterozygotes, DD homozygotes. While the distribution of ACE polymorphism in control subjects was 33%, 43%, 24%, the distribution of it in Facial nerve palsy patients was 32%, 50%, 18%(II, ID, DD). Thus, there was no significant different between the control and Facial nerve palsy groups. Conclusions : we conclude that there is no significant association between ACE gene polymorphism and Facial nerve palsy in Korean population. However, the findings of this study need to be confirmed in more patients and further studies. Additional epidemiologically based studies of the effects and relationship between ACE or other genes and lifestyles with regard to Facial nerve palsy is required.

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