http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : Bumpus (검색결과 3 건)
- 무료
- 기관 내 무료
- 유료
-
Synthesis of Ileu^5, Ala^8-Angiotensin Ⅱ : Ocapeptide
Park, Won-Kil,Bumpus, F. M. 慶北大學校 1962 論文集 Vol.6 No.-
Ileu^5,-Angiotensin Ⅱ 卽 Octapeptide의 Amino酸의 結合順序는 다음과 같다. Asp-Arg-Val-Tyr-Ileu-His-Pro-Phe이다. 이것이 合成方法, 經路 及 藥理作用 等은 F. M. Bumpus 及 그의 共同硏究員들에 依하야 發表되였든 것이다. 그러나 8位置의 Phenylalanine의 Phenyl基를 除去한 Alanine로된 所謂 Ala^8-Angiotensin Ⅱ의 關한 合成, 經路, 藥理作用 等이 未發表되여 있으므로 本人들은 다음과 같은 條件下에 合成했든 것이다. 卽 N-terminal와 C-terminal의 Protective group로서 各各 Carbobenzoxy基, P-Nitrobenzy1基로 擇하고 特히 Histidine의 Imidazol group는 benzy1基로 protecte했다. 合成中基體인 tetrapeptide,〔Ileu-(I-B)His-Pro-Phe〕는 結晶體를 得하지 못했기 때문에 元素分析은 不可能 했으며 直接 Hexbpeptile로 合成했다. 最終 生成物인 free Octapeptide 收量이 적기때문에 역시 元素分析代身에 Amino酸分析과 Chromatography, 及 Electrophoresis 等으로 確認했던 것이다. 藥理作用은 Ileu^5-Angiotensin Ⅱ과 類似했으며, 本論文에서는 主로 合成에 關해서 發表했다. 使用한 Amino酸은 全部 L-型의다. An Ileu^5-Angiotensin Ⅱ was synthesyzed by F. M. Bumpus et al. The synthesis of the Ileu^5, Ala^8-Angiotensin Ⅱ using by mixed anhydride and azide methods, is described here. Tetrapeptide. HBr; Ileu-(I-B_z) His-Pro_Ala_OBzNO_2. HBr was not crystal or solid and very hygroscopic material. An imidazol group of histidine was protected with benzyl group and a C-terminal blocking group, p-nitro-benzyl ester. The final product was determined by amino acids analysis.
-
Synthesis of Isoleucyl^5-Alanyl^7-Angiotensin Ⅱ
Seu, Jung-Hwn,Smeby, Rbert R.,Bumpus, F. Merlin 慶北大學校 1962 論文集 Vol.6 No.-
The octapeptide isoleucyl -alanyl -angiotensin Ⅱ has been synthesized in order to study further the significance of structure at the C-terminal end of angiotesin Ⅱ for biological activity. This replacement of proline, in position 7 of angiotensin Ⅱ, by alanine, greatly reduced the pressor and oxytocic activites of the peptide. This marked loss of activity, by merely removing two methylene groups of the proline ring, may be caused by a changing of the confermation at the C-terminus of the peptide. Addition of urea to an aqueous solution of angiotensin Ⅱ greatly reduces its myotrpohic action and also causes a marked reduction in degree of order showing bythe peptide as studied, by optical rotatory dispersion. From this it follows that the conformation of the peptide is an important factor for the myotrophic activity. Isoleucyl -angiotensin Ⅱ, the octapeptide L-aspartyl-L-arginyl-L-valyl-L_tyrosyl-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanine, exhibits marked specificty of structure at the C-terminus for pressor and myotrophic activities. Removal of L-phenylalanine or only the aromatic ring of this amino acid destroys the biological activities of the peptide. Conversion of the C-terminal carboxyl group to an amide group causes some reduction in biological activities. The phenolic ring of tyrosine and the imidazole ring of histidine have also been reported to be essential for the biological activities of the peptide. A conformation recently suggested for angiotensin Ⅱ , based on the assumption it will form anα-helix to the greatest extent possible, will explain all physical and biological data presently known for this peptide. In this conformation the groups essential for biological activity are all arranged in close proximity and on the same side of the molecule. Since rupture of the aliphatic ring of proline would change the stucture at the C-terminus of the peptide and would alter the relative position of these essential groups, we have replaced proline in angiotensin Ⅱ with alanine by the preparation of isoleucyl -ananyl angiotensin Ⅱ.
-
SYNTHESIS OF ALANYL^4-ISOLEUCYL^5-ANGIOTENSIN Ⅱ
Seu, Jung-Hwn,Robert R. Smeby,F. M. Bumpus 慶北大學校 1962 論文集 Vol.6 No.-
Resent studies on analogues and homologues of angiotensin I, the pressor octapeptide L-aspart1-L-arginyl-L-valyl-L-tyrosyl-L-histidyl-L-prolyl-L-phenylalanine, have shown the two amino acids with aomatic rings are important to biological activity. Removal of the aromatic ring of phenylalanine greatly reduced pressor activity. The peptide without the phenolic hydroxy group of tyrosine, phenylalanine angiotensin, has only 2 to 10% of the activity of the parent octapeptide. The two aromatic side gropes are positioned, very close to each other in a conformation recently suggested for angiotensin I.
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
