• 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.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2001.10a
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• pp.97-98
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• 2001

순환기계 질병의 원인이 되는 동시에 뇌출혈, 심장병 및 신장병 등과 합병증으로 나타날 경우 치사율이 매우 높은 만성 퇴행성 질환인 고혈압의 90％ 이상을 차지하는 본태성 고혈압은 정상적인 혈압을 유지하는 기구들이 천천히 붕괴되어 진행되는 질병이다(Frohlich, 1982). 이러한 본태성 고혈압의 원인 중에서 reninㆍangiotensin계가 혈압조절에 매우 중요한 역할을 한다고 알려지고 있다(Saxena, 1992). 즉, angiotensinogen이 renin의 분해를 받아서 angiotensin I을 생성하는데, 이는 angiotensin converting enzyme(ACE)에 의하여 COOH 말단의 dipeptide가 절단되어 강력한 혈관수축작용을 하는 angiotensin II를 생성한다. (중략)

• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.23-23
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• 1996

A working molecular model of the angiotensin II type 1 receptor is built based on the seven transmembrane helix structure of the recently refined bacteriorhodopsin atomic coordinates. A multiple copy simultaneous search (MCSS) method is used to search the pharmacophore of angiotensin on the surface of the receptor. Multiple copies of amino acid fragments and organic functional groups are scattered around the possible binding site and the time dependent. (omitted)

• Journal of Life Science
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• v.8 no.3
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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.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2002.10a
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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)

• 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.

• Korean Journal of Pharmacognosy
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• v.14 no.4
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• pp.145-148
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• 1983

Angiotensins and bradykinin play important roles in blood pressure regulation and in other physiological and pathological conditions. The present work is aimed to investigate potential antagonists against either angiotensin or bradykinin from plant sources. Each methanol extract of selected 25 plants was solvent fractionated to three fractions. The effects of total of 75 plant samples against the contractions induced by angiotensin I or bradykinin in rat ileum were measured. The results are summarized.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.94-94
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• 1993

Angiotensin 전환효소 억제제를 재료로하여 다기관 협동을 통한 시판 후 조사방법론을 개발하고, 아울러 Angiotensin 전환효소 억제제 투여시 나타나는 기침의 발생율과 이와 관련된 요인을 밝히고자 시판 후 조사를 시도하였다. 방법: 1992년 2월부터 1992년 10월까지 11개 병원 가정의학과를 방문하여 Angiotensin 전환효소 억제제를 투여한 고혈압 환자 348명을 연구대상으로 하였다. 이중 남자가 147명, 여자가 201명이었으며, 연령별로는 39세이하 38명, 40-54세 156명, 55세 이상이 154명이었다. 최초 약물투여 후 2, 4, 8, 12주에 추적 관찰하였으며, 기침의 발생율은 PC-SAS 6.04를 이용하여 Kaplan-Meier 방법과 Log-Rank 방법으로 분석하였다.

• YAKHAK HOEJI
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• v.45 no.1
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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.

• Archives of Pharmacal Research
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• v.17 no.6
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• pp.405-410
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• 1994

The present study was undetertaken to demonstrate whether or not angiotensin II activates a phopholipase D in rabbit kidney proximal tubule cells. By measuring the formation of [$^3H$] phosphatidic acid and [$^3H$]diacylglycerol. This result suggests that some phosphatidic acid seems to be formed directly from phosphatidylcholin by the action of phopholipase D, not from the action of diacylglycerol kinase on the diacylglycerol. In addition the other mechanisms by which phospholipase D is activated was examined. We have found that phospholipase D was activited by extracellular calium ion. It has also been shown that angiotensin II may activate phosphoilpase D through protein kinase C-independent pathway.