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公开(公告)号：KR100318553B1
公开(公告)日：2002-05-13
申请号：KR1019980044601
申请日：1998-10-23
Applicant: 한국과학기술연구원
IPC: C07K5/08
Abstract: 본 발명은 안지오텐신-I-전환효소(angiotensin-I-converting enzyme:ACE)의 억제활성을 갖는 인간 알파s1 카세인 유래의 신규 생리활성 펩타이드 Leu-Gln-Trp 및 그의 고혈압 치료를 위한 용도에 관한 것으로 인간 알파s1 카세인의 168-170번째 펩타이드인 Leu-Gln-Trp를 합성한 후 역상 고속 액체 크로마토그라피(Reverse Phase-High Performance Liquid Chromatography:RP-HPLC)를 사용하여 상기 펩타이드의 ACE 억제활성을 분석 및 정량한 결과, 상기 펩타이드는 ACE 억제활성이 있어 고혈압 치료제로 유용한 뛰어난 효과가 있다.
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Patent Agency Ranking
公开(公告)号：KR100266753B1
公开(公告)日：2000-09-15
申请号：KR1019980006237
申请日：1998-02-26
Applicant: 한국과학기술연구원
Abstract: PURPOSE: Provided is E. coli transformant that is transformed with human alpha S1 casein gene, thereby the human alpha S1 casein can be effectively produced, so that it can be used in studies about the functions of the human alpha S1 casein. CONSTITUTION: The transformant E. coli BL21(DE3)/pHalpha S1C2(KCTC 8867P) is prepared by the steps of: amplifying cDNA of human alpha S1 casein by PCR using probes and treating it with endonucleases such as Ndel/SaII and Ndel/XhoI; inserting the amplified cDNA of human alpha S1 casein into plasmid pET 22b(+) to construct pHalpha S1C1 and pHalpha S1C2; and transforming E. coli BL21 with pHalpha S1C1 and pHalpha S1C2. The mino acid sequence of human alpha S1 casein is analyzed by the steps of: incubating E. coli BL21(DE3)/pHalpha S1C2(KCTC 8867P) and collecting the cells; crushing the cells, and followed by centrifuging and separating it into a water-soluble fragment and a water-insoluble fragment; subjecting the fragments to Ni-NTA column chromatography; and analyzing the amino acid sequence of the separated and purified human alpha S1 casein with a protein sequencer.
Abstract translation: 目的：提供用人α1S酪蛋白基因转化的大肠杆菌转化体，从而可以有效地产生人α1S酪蛋白，从而可用于关于人α1S酪蛋白的功能的研究。 构成：通过以下步骤制备转化体大肠杆菌BL21（DE3）/ pHalpha S1C2（KCTC 8867P）：通过使用探针通过PCR扩增人α1S酪蛋白的cDNA并用核酸内切酶如Ndel / SaII和NdeI / XhoI ; 将人α1S酪蛋白的扩增cDNA插入质粒pET223（+）中以构建pHalpha S1C1和pHalpha S1C2; 并用pHalpha S1C1和pHalpha S1C2转化大肠杆菌BL21。 通过以下步骤分析人α1S酪蛋白的微型酸序列：温育大肠杆菌BL21（DE3）/ pHalpha S1C2（KCTC 8867P）并收集细胞; 粉碎细胞，然后离心分离成水溶性片段和水不溶性片段; 将片段进行Ni-NTA柱色谱; 并用蛋白测序仪分析分离和纯化的人α1S酪蛋白的氨基酸序列。
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公开(公告)号：KR1020000026872A
公开(公告)日：2000-05-15
申请号：KR1019980044601
申请日：1998-10-23
Applicant: 한국과학기술연구원
IPC: C07K5/08
CPC classification number: A61K38/06 , C07K5/0808
Abstract: PURPOSE: A peptide useful as antihypertensives is provided which has a strong ACE inhibiting activity. CONSTITUTION: A physiological active peptide of Leu-Gln-Trp from human alpha s1 casein is provided. Thus, 5 mM of Hip-His-Leu is dissolved in 0.1 M of borate buffer solution, followed by addition of 100 micro liter 1N hydrochloride solution and 5 micro liter of 5 mU ACE at 37°C for 30 minutes. 1 N-sodium chloride solution is reacted with the obtained solution to terminate the reaction. ACE inhibiting activity of Leu-Gln-Trp peptide is analyzed by RP-HPLC.
Abstract translation: 目的：提供可用作抗高血压药物的肽，其具有强烈的ACE抑制活性。 构成：提供了人α1酪蛋白的Leu-Gln-Trp的生理活性肽。 因此，将5mM的Hip-His-Leu溶解于0.1M硼酸盐缓冲溶液中，然后在37℃下加入100微升1N盐酸溶液和5微升5mU ACE 30分钟。 使1N氯化钠溶液与所得溶液反应终止反应。 通过RP-HPLC分析Leu-Gln-Trp肽的ACE抑制活性。
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公开(公告)号：KR1019990073772A
公开(公告)日：1999-10-05
申请号：KR1019980006887
申请日：1998-03-03
Applicant: 한국과학기술연구원
IPC: C07K14/81
Abstract: 본 발명은 대장균에서 발현한 재조합 인체 알파s1 카제인을 트립신으로 처리하여 분리한 안지오텐신-I-전환효소(ACE) 억제 활성을 갖는 인간 알파s1 카제인 유래의 신규한 생리활성 펩티드에 관한 것이다.
본 발명의 인체 알파 s1 카제인 유래의 생리활성 펩티드는 8~11번의 펩티드 Tyr-Pro-Glu-Arg, 136~143번의 펩티드 Tyr-Tyr-Pro-Gln-Ile-Met-Gln-Tyr과 164~170번의 펩티드 Asn-Asn-Val-Met-Leu-Gln-Trp로서 ACE에 대하여 각각 억제활성이 있는 뛰어난 효과가 있다.-
公开(公告)号：KR1019990071038A
公开(公告)日：1999-09-15
申请号：KR1019980006237
申请日：1998-02-26
Applicant: 한국과학기술연구원
Abstract: 본 발명은 인간 알파s
1 카제인을 발현시키는 플라스미드 pHαs
1 C2를 제작하고 이 플라스미드로 카르복시 말단에 6개의 히스티딘이 붙은 인간 알파s
1 카제인을 발현시킨 후 Ni-NTA 칼럼 크로마토그라피로 분리정제하므로써 순수하게 정제된 인간 알파s
1 카제인을 얻을 수 있는 뛰어난 효과가 있다.-
公开(公告)号：KR100294244B1
公开(公告)日：2001-07-12
申请号：KR1019980006887
申请日：1998-03-03
Applicant: 한국과학기술연구원
IPC: C07K14/81
Abstract: PURPOSE: Provided are a novel bioactive peptide containing inhibiting activity of angiotensin-I-converting enzyme(ACE) and its usage for curing hypertension. Particularly, the bioactive peptide is manufactured by separating an alpha s1 casein from cDNA library of human mammary gland and expressing it in E.coli, wherein 6 of histidines are added to C terminal in order to easily purify alpha s1 casein. CONSTITUTION: A human alpha s1 casein is expressed in E.coli and purified. And then, recombinant human alpha s1 casein is decomposed into trypsin. Thereafter, ACE inhibitory peptide is separated by using high performance liquid chromatography(HPLC). Next, an amino acid sequence of the selected peptide is analysed and a molecular weight thereof is measured. Finally, an ACE inhibiting activation of peptide is analyzed quantitatively.
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