• 제목/요약/키워드: angiotensin-converting

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

  • 김현우;이중헌
    • KSBB Journal
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    • 제28권2호
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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%).

대구의 간 단백질의 효소적 가수분해물로부터 안지오텐신 I 전환효소 저해 펩타이드의 분리.정제 및 특성 (Purification and Characterization of Angiotensin I Converting Enzyme lnhibitory Peptides from Enzymatic Hydrolysate of Cod Liver Protein)

  • 최영일;박표잠;최정호;변희국;정인철;문성훈;김세권
    • 생명과학회지
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    • 제10권2호
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    • pp.140-149
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    • 2000
  • In order to utilize marine processing waste which would normally be discarded, cod liver protein was hydrolysed by ${\alpha}$-chymotrysin, and the hydrolysate was investigated for the new angiotensin I converting enzyme (ACE) inhibitor. Thy hydrolysate was separated into three major types, with molecular weight cut-off (MWCO) values less than 10 kDa, 5 kDa and 1 kDa of ultrafiltration membranes, respectively. ACE inhibitory peptides were isolated from the fractions passed through MWCO 1 kDa membrane, and purified by using ion-exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-15 column, and HPLC on an ODS column. The purity was identified with capillary electrophoresis. The amino acid sequences of two peptides were Met-Ile-Pro-Pro-Tyr-Tyr (IC50=10.9 ${\mu}$M) and Gly-Leu-Arg-Asn-Gly-Ile (IC50=35.0 ${\mu}$M)

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특발성 간질성 폐렴 환자에서 임상적 지표와 혈청 Angiotensin Converting Enzyme(ACE) 및 Angiotensin II와의 관계 (The Relationship of Serum Angiotensin Converting Enzyme(ACE), Angiotensin II and Clinical Markers in the Idiopathic Interstitial Pneumonia)

  • 경선영;한혜숙;송석호;황준규;임영희;안창혁;박계영;박정웅;정성환;하승연;이재웅
    • Tuberculosis and Respiratory Diseases
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    • 제52권5호
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    • pp.506-518
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    • 2002
  • 연구배경 : 특발성 간질성 폐렴에서 폐섬유화를 일으키는 주된 세포인 섬유아세포를 활성화시키면서 폐포 상피 세포의 세포사멸에 큰 역할을 하는 것으로 알려진 angiotensin II와 antiotensin converting enzyrne(ACE) 혈청 수치를 측정하여, 이들과 환자의 폐기능, 호흡곤란 정도, 기관지폐포세척액에서 세포 분획과의 관계를 알아보고자 하였다. 방 법 : 저자들은 가천의대 길병원에서 특발성 간질성 폐렴으로 진단된 23명의 환자를 대상으로 하였다. 이들 모두에서 내원 당시 혈청 ACE와 angiotensin II를 측정하여 각각을 증가군과 비증가군으로 나누었으며 환자들의 폐기능 검사, 호흡곤란 정도 지수, 기관지폐포세척술상 세포 분획을 측정하여 비교하였다. 결 과 : 전체 환자 23명에서 혈청 ACE 증가군은 14명, 비증가군은 9명이었고, angiotensin II의 경우 증가군이 14명, 비증가군이 9명이였다. DLCO%의 경우 angiotensin II 비증가군이 $64.0{\pm}19.8%$, 증가군이 $51.6{\pm}18.7%$로 증가군에서 유의한 수준으로 감소된 소견을 보였다(p=0.021). 결 론 : 특발성 간질성 폐렴 환자 중 혈청 angiotensin II의 비정상적인 증가가 있는 군에서 폐확산능의 유의한 감소가 보여 angiotensin II의 증가가 폐 섬유화의 진행 과정에서 중요한 역할을 할 것으로 생각되며, 그 기전에 대한 연구가 지속적으로 필요할 것으로 사료된다.

멸치 가공선 자숙액 pepsin 가수분해물의 angiotensin 전환효소 저해작용

  • 지청일;이지혜;박덕천;구연숙;박재홍;박영호;김인수;김선봉
    • 한국어업기술학회:학술대회논문집
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    • 한국어업기술학회 2001년도 추계 수산관련학회 공동학술대회발표요지집
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    • pp.171-172
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    • 2001
  • 체내에 널리 분포되어 있는 angiotensin 전환효소(angiotensin converting enzyme, ACE ; peptidyldipeptide hydrolase, EC 3.4.15.1)는 angiotensinogen이 renin의 특이적 분해를 받아서 생성된 불활성형인 angiotensin I의 말단 dipeptide(His-Leu)를 절단하여 octapeptide인 활성형의 angiotensin II로 전환시키며, 이렇게 생성된 angiotensin II는 직접적으로 혈압상승 작용을 하거나 adrenal로부터 sediumretaining steroid hormone인 aldosterone의 유리를 촉진시켜 체내 나트륨을 저류시킨다. (중략)

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Upregulation of Renin-angiotensin, Endothelin and C-type Natriuretic Peptide in Rat Glomerulus with Bilateral Ureteral Obstruction

  • Bae, Eun-Hui;Kim, Soo-Wan
    • The Korean Journal of Physiology and Pharmacology
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    • 제10권6호
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    • pp.343-347
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    • 2006
  • The present study was designed to investigate the effects renin-angiotensin-aldosterone system (RAAS), endothelin (ET) and local natriuretic peptide (NP) system for glomerulopathy induced in the experimental bilateral ureteral obstructive rats. Sprague-Dawley male rats ($200{\sim}220g$ body weight) were bilaterally obstructed by ligation of the proximal ureters for 24 hours. Control rats were treated in the same ways, except that no ligature was made. The glomeruli were isolated from cortex by graded sieve methods, and the mRNA expressions of local renin-angiotensin system (RAS), aldosterone synthase (CYP11B2), endothelin-1 (ET-1) and NP system were determined by real-time polymerase chain reaction. Following the bilateral ureteral obstruction, the mRNA expressions of renin, angiotensin converting enzyme 1 as well as ET-1 were increased, while that of angiotensin converting enzyme 2 was not changed. The expressions of CYP11B2 and angiotensin II receptors were not changed. C-type natriuretic peptide (CNP) expression was increased, while its receptors (natriuretic peptide receptor-B) were not changed. We suggest that the upregulation of local RAS and ET playa role in the progressive glomerular injury, and that the enhanced CNP activity also plays a compensatory role in obstructive uropathy in the glomerulus.

Angiotensin 변환 효소 억제제인 Captopril 유도체들의 구조와 활성관계 연구: 수용액상의 분자동력학적 연구의 중요성 (Structure-Activity Relationships Study of Angiotensin Converting Enzyme Inhibitor Captopril Derivatives: Importance of Solution Moleculnr Dynamics Study)

  • 지명환;윤창노;진창배;박종세
    • Biomolecules & Therapeutics
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    • 제2권1호
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    • pp.34-38
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    • 1994
  • In order to investigate the structure-activity relationships of the stereoisomers of angiotensin converting enzyme inhibitors, captopril and its derivatives were selected as model compounds. In vitro enzymatic activities of them depend on the symmetry at the asymmetric carbons. Especially, the alanyl carbon should have the S configuration to be biologically active. But the demethylated captopril having the achiral carbon also shows the activity although it is less active than captopril. Seven stereoisomers of captopril and its derivatives were chosen and their acidic and ionic forms were used for molecular dynamics simulations. Four computer simulations were practiced for each model compound in order to obtain the good condition for simulation to explain the experimental structure-activity relationships. From the computer simulation results, relativistic movements of three well-known pharmacophoric sites, carboxylate carbon, carbonyl oxygen, and sulfur atoms, were analyzed. Good results were obtained from the aqueous solution molecular dynamics simulation with ionic forms of model compounds. Active model compounds have the pharmacophoric areas of 6.08 to 6.38 $\AA$$^2$and the similarity in the geometrical data. But inactive ones have the largely deviated values of 4.51 to 4.87 $\AA$$^2$from those of active ones.

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오징어(Todarodes pacificus) 껍질로부터 Angiotensin I 전환효소 저해 펩티드의 분리 정제 (Purification of Angiotensin I-Converting Enzyme Inhibitory Peptide from Squid Todarodes pacificus Skin)

  • 이정권;전중균;변희국
    • 한국수산과학회지
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    • 제44권2호
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    • pp.118-125
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    • 2011
  • In this study, an angiotensin I-converting enzyme (ACE) inhibitor from squid skin was purified and characterized. Squid (Todarodes pacificus) skin protein isolates were hydrolyzed using six commercial proteases: alcalase, ${\alpha}$-chymotrypsin, neutrase, papain, pepsin, and trypsin. The peptic hydrolysate had the highest ACE inhibitory activity. The ACE inhibitory peptide was purified using Sephadex G-25 column chromatography and reverse phase high-performance liquid chromatography (HPLC) with a $C_{18}$ column. The purified ACE inhibitory peptide was identified and sequenced, and found to consist of seven amino acid residues: Ser-Ala-Gly-Ser-Leu-Val-Pro (657Da). The $IC_{50}$ value of the purified ACE inhibitory peptide was 766.2 ${\mu}M$, and Lineweaver-Burk plots suggested that the purified peptide acts as a noncompetitive ACE inhibitor. These results suggest that the ACE inhibitory peptide purified from the peptic hydrolysate of squid skin may be of benefit in developing antihypertensive drugs and functional foods.

참치 자숙액의 Angiotensin 전환효소 저해작용 (Angiotensin Converting Enzyme Inhibitory Activity of Skipjack/Yellow Tuna Cooking Broth)

  • 여생규;이태기;안철우;김인수;구연숙;박영호;김선봉
    • 생명과학회지
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    • 제8권3호
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    • pp.312-317
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    • 1998
  • This study was designed to investigate the angiotensin convertin enzyme (ACE) inhibitory activity of skipjack/yellowpin tuna cooking broth. The cooking broth was pretreated with membrane filter (MW cut-off 5,000) to obtain the peptide fraction with ACE inhibition. the crude peptides fractionated with Amberlite IR-120 ($H^{+}$ form and followed by Bio-gel P-2, were separated into nine fractions (T-1 to T-9). The maximum inhibitory activity was observed in the fraction T-4 ($IC_{50}$ value, 0.619mg/ml). The abundant amino acids obtained from active fraction T-4 were phenylaanine, leucine and glutamic acid.

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Angiotensin I Converting Enzyme Inhibitor Derived from fermented Mussel, Mytilus edulus

  • Je, Jae-Young;Park, Pyo-Jam;Byun, Hee-Guk;Kim, Se-Kwon;Kim, Jong-Bae;Chang, Soo-Hyun
    • 한국어업기술학회:학술대회논문집
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    • 한국어업기술학회 2002년도 추계 수산관련학회 공동학술대회발표요지집
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    • pp.191-192
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    • 2002
  • Angiotensin I converting enzyme [EC 3.4.15.11 (ACE) is important in the maintenance of blood pressure. The enzyme removes histidyl-leucine from angiotensin I to form the blood-vessel-constricting octapeptide, angiotensin II, and degrades vasodilative bradykinin in blood vessels and stimulates e release of aldosterone in the adrenal cortex. (omitted)

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SHR에 있어 Enalapril의 ACE억제효과에 대한 Ginkgo biloba Extract(EGb 761)의 영향 (Effects of Ginkgo biloba Extract (EGb 761) on the Enalapril-induced ACE Inhibition in SHRs)

  • 이영미;염윤기;신완균;손의동;안형수
    • 약학회지
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    • 제45권1호
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    • pp.93-100
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    • 2001
  • Drug inetraction between of enalapril-induced angiotensin converting enzym) inhibitory effect and Ginkgo biloba Ext.-induced antioxidant action was evaluated in spontaneously hypertensive rats. Combination treatment of enalapril (20 mg/kg/day p.o.) and Ginkgo biloba Ext. (60 mg/kg/day, p.o.) for 6 weeks in drinking water to SHRs resulted the inhibition of ACE activity in lung tissue, angiotensin I-induced pressure response and plasma angiotensin II concentration as similar to enalapril alone treatment. But these effects were sustained after 1 week withdrawal of enalapril and Ginkgo biloba Ext. co-administeration. Also, coadministered group did not increase the concentration of bradykinin in lung tissue, which were different from enalapril alone treated group. Co-administration of enalapril and Ginkgo biloba Ext. inhibited the hemolysis induced by UV B type, even Ginkgo biloba Ext. alone treated group did not. These results suggested that Ginkgo biloba Ext. sustained ACE inhibitory effect and reduced the inhibitory effect of bradykinin inactivation induced by enalapril, meanwhile, enalapril increased the antioxidant effect of Ginkgo biloba Ext.

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