• BMB Reports
• /
• 제35권2호
• /
• pp.239-243
• /
• 2002

Angiotensin I that converts the enzyme (ACE) inhibitory peptide, Gly-Pro-Leu, previously purified and identified from the Alaskan pollack skin gelatin hydrolysate, were synthesized. In addition, the peptides Gly-Leu-Pro, Leu-Gly-Pro, Leu-Pro-Gly, Pro-Gly-Leu, Pro-Leu-Gly, Gly-Pro, and Pro-Leu, which consisted of glycine, proline, and leucine, were synthesized by the solid-phase method. The $IC_{50}$ values of each tripeptide - namely Leu-Gly-Pro, Gly-Leu-Pro, Gly-Pro-Leu, Pro-Leu-Gly, Leu-Pro-Gly, and Pro-Gly-Leu - were 0.72, 1.62, 2.65, 4.74, 5.73, and $13.93{\mu}M$, respectively. The ACE inhibitory activity of these tripeptides was higher than that of dipeptides, such as Gly-Pro and Pro-Leu with $IC_{50}$ values of 252.6 and $337.3\;{\mu}M$, respectively. Among the tripeptides, Leu-Gly-Pro and Gly-Leu-Pro had higher inhibitory activity than Gly-Pro-Leu that was isolated from the Alaskan pollack skin gelatin hydrolysate. Among the different types of tripeptides that were examined, the highest ACE inhibitory activity was observed for Leu-Gly-Pro. It had the leucine residue at the N-terminal and proline residue at the C-terminal.

• 약학회지
• /
• 제28권6호
• /
• pp.313-319
• /
• 1984

Phenylurea, phenylthiourea, benzylcarbamate and toluenesulfonate of L-alanyl-L-proline(comp. $3{\sim}6$) were synthesized and their effects against angiotensin-converting enzyme (ACE) were tested. Comp. 3 showed only mild inhibitory activities against ACE while comp. $4{\sim}6$ were inert indicating that those functional groups were not suitable for interactions with ACE. Ortho-hydroxy- or ortho-carboxy-benzamide of proline (comp. 7) and phenylalanine (comp. 8 and 9) were also tested. Of the benzamides, ortho-hydroxy function was unsuitable to exert inhibitory activities against ACE. Ortho-carboxy group of 9 seemed to have mild interactions with active site of ACE possibly because of the shorter distance between the amide and ortho-carboxyl group of the compound than the corresponding two active sites of the enzyme.

• 한국어업기술학회:학술대회논문집
• /
• 한국어업기술학회 2002년도 추계 수산관련학회 공동학술대회발표요지집
• /
• pp.90-91
• /
• 2002

The angiotensin converting enzyme (ACE) generates the powerful vasoconstrictor angiotensin II by removing the C-terminal dipeptide from the precursor decapeptide angiotensin I (1). The enzyme also inactivates the vasodilator bradykinin (2). There have been many studies on ACE inhibitory substances as functional in food, and ACE inhibitory peptides were isolated (3-5). (omitted)

• Asian Pacific Journal of Cancer Prevention
• /
• 제15권24호
• /
• pp.10691-10695
• /
• 2015

Background: Association of angiotensin converting enzyme (ACE) gene polymorphisms with lung cancer susceptibility remains uncertain and varies with ethnicity. Northeast India represents a geographically, culturally, and ethnically isolated population. The area reports an especially high rate of tobacco usage in a variety of ways of consumption, compared with the rest of the Indian population. Materials and Methods: We conducted a population based case control study in two major high risk region for lung cancer from Northeast India. A total of 151 consecutive lung cancer cases diagnosed histopathologically and equal numbers of controls were recruited with record of relevant sociodemographic information. Blood samples were collected and processed to identify ACE gene polymorphism. Results: Significantly higher (40.4 % vs 29.1%, OR=1.97, CI=1.04-3.72; p=0.037) prevalence of the ACE II genotype was observed among lung cancer cases. Smoking was significantly associated with increased risk of lung cancer (OR=1.70, CI=1.02-2.81; p=0.041). An enhanced risk was also observed for interaction of ACE II genotype with tobacco smoking (OR=4.09, CI=1.51-11.05; p=0.005) and chewing (OR=3.68, CI=1.22-11.13; p=0.021). Conclusions: The present study indicates significant association s of the ACE II genotype with lung cancer in high risk Northeast India.

• 한국어업기술학회:학술대회논문집
• /
• 한국어업기술학회 2001년도 추계 수산관련학회 공동학술대회발표요지집
• /
• pp.97-98
• /
• 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)

• Applied Biological Chemistry
• /
• 제40권1호
• /
• pp.39-42
• /
• 1997

돼지혈액의 혈장으로부터 ACE 저해제들을 분리 정제하였다. 돼지 도축혈액을 먼저 혈액응고방지제를 첨가한후 원심분리에 의해 혈장과 혈구로 분리한 다음 혈장단백질을 최종농도 4% TCA로 침전시켰다. ACE 저해제들은 TCA 상등액과 혈장단백질 가수분해물로부터 한외여과, 겔여과크로마토그라피, 역상고속액체크로마토그라피 방법으로 분리되었는데 $IC_{50}4값들이 각각 $2\;{\mu}M,\;23\;{\mu}M$로 측정되었다.

• 운동영양학회지
• /
• 제24권1호
• /
• pp.24-28
• /
• 2020

[Purpose] Recent studies have demonstrated a probable association between ACE I/D polymorphism and obesity. Thus, this study aimed to investigate whether ACE I/D polymorphism influenced the susceptibly of developing obesity in Korean adults. [Methods] A total of 353 healthy Korean adults aged between 30 and 82 years were recruited, including 157 males and 196 females. Among the participants, 103 (29.2 %) were classified as normal (BMI < 23 kg/m²), 117 (33.1 %) as overweight (23 kg/m² ≤ BMI < 25 kg/m²), and 133 (37.7 %) as obese (BMI ≥ 25 kg/m²). ACE polymorphism (rs1799752) analysis was performed using the MGB TaqMan® SNP Genotyping assay with 3 types of primers and 2 types of probes. The distributions of the ACE genotypes and allele frequencies were analyzed among the three groups using the Hardy-Weinberg equilibrium, chi-square tests, and multiple regression analysis. [Results] The distribution of the ACE genotypes were as follows: normal [II: n=38 (36.9 %), ID: n=46 (36.8 %), DD: n=19 (18.4 %)], overweight [II: n=43 (36.8 %), ID: n=55 (47.0 %), DD: n=19 (16.2 %)], and obese [II: n=41 (30.8 %), ID: n=76 (57.0 %), DD: n=16 (12.0 %)]. Unexpectedly, the I allele, rather than the D allele, was common in the obese group. [Conclusion] ACE I/D polymorphism is not associated with BMI in Korean adults. Thus, it is unlikely to be a powerful candidate gene for obesity in Korean adults.

• 한국식품영양과학회지
• /
• 제36권12호
• /
• pp.1511-1516
• /
• 2007

두충의 기능성 식품으로서 이용 가능성을 평가하기 위하여, 두충의 항고혈압 활성 물질을 분리 및 확인하였고, 각 부위별(잎, 껍질, 줄기) 추출물의 관련물질의 함량 및 ACE 저해활성을 조사하였다. 두충에서 분리한 항고혈압성 물질로 추정되는 8A는 순도 95.64%의 pinoresinol-4,4'-di-O-${\beta}$-D-glucoside(PDG)로서 자연건조 및 볶은 껍질에서 가장 높았으며, 각각 135.13 mg%와 163.67 mg%였다. 또한 두충 추출물의 ACE 저해활성은 10 mg/mL 농도로 처리하였을 때 볶은 잎, 자연건조 껍질 및 볶은 껍질에서 각각 77.56%, 75.73%, 75.73%로 높은 활성을 나타내었으며, 줄기는 상당히 낮게 나타났다. 두충에서 분리한 PDG를 1 mg/mL 처리할 때, ACE 저해활성은 91.87%로서 $Enalapril^{(R)}$의 97.06%보다는 조금 낮았지만, $Captopril^{(R)}$의 90.32% 보다는 약간 높은 항고혈압 활성을 나타내었다.

• 한국응용약물학회:학술대회논문집
• /
• 한국응용약물학회 1993년도 제2회 신약개발 연구발표회 초록집
• /
• pp.121-121
• /
• 1993

Angiotensin Converting Enzyme (ACE)의 효과적인 억제제를 합성하기 위하여 ketomethylene dipeptide isoster와 2-isoxazoline dipeptide isoster를 얻는 방법을 확립하였다. 상기 등입체성 분자들은 아미노산으로부터 유도된 아미노 니트릴 옥사이드의 고리더함반응을 이용하여 효율적으로 합성하였다. 얻어진 이 화합물로부터 ACE 억제제 후보물질 (1, 2)의 합성이 연구되고 있다.

• 한국어업기술학회:학술대회논문집
• /
• 한국어업기술학회 2002년도 추계 수산관련학회 공동학술대회발표요지집
• /
• pp.191-192
• /
• 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)