- 고상법에 의한 Bradykinin 유사물의 합성(III)
- ㆍ 저자명
- 최청,성태수,Choi. Cheong,Sung. Tae-Soo
- ㆍ 간행물명
- 한국생화학회지
- ㆍ 권/호정보
- 1984년|17권 3호|pp.339-345 (7 pages)
- ㆍ 발행정보
- 생화학분자생물학회
- ㆍ 파일정보
- 정기간행물| PDF텍스트
- ㆍ 주제분야
- 기타
개량된 반응기구를 사용하여 고상법으로 ($Tyr^5$), ($Tyr^8$), ($Tyr^5$, $Tyr^8$) 및 ($Trp^8$) bradykinin 유사물을 합성하였으며 그 수득률은 58.6~68.2%였다. Coupling은 dicyclohexylcarbodiimide에 의하여 이루어졌으며 HBr로 cleavage 한 각 펩티드는 Sephadex G-25와 carboxymethyl cellulose chromatography에 의해 분리하였다. 이들의 순도 결정은 종이 및 박충 크로마로그래피, 융점, 아비노산분석 및 생물학적 활성을 측정하였다. ($Try^8$) bradykinin은 bradykinin을 표준물질로하여 백쥐의 혈압강하에서 bradykinin보다 약 1.3배의 활성을 나타내었다. Endopeptidase인 $alpha$-chymotrypsin과 exopeptidase인 carboxypeptidase A와 leucine aminopeptidase를 사용하여 이들의 펩티드 분해 실험을 하였다. $alpha$-Chymotrypsin과 carboxypeptidase의 작용은 펩티드를 빠르게 분해시켰으나 leucine aminopeptidase는 약간 느리게 분해되었다.
Synthesis of ($Tyr^5$), ($Tyr^8$), ($Tyr^5$, $Tyr^8$) and ($Trp^8$) analogues of bradykinin was carried out by solid phase method. The yield range from 58.6 to 68.2% owing to an improved reaction vessel. Coupling was performed by dicyclohexylcarbodiimide. After cleavage with dried HBr the peptides were purified by Sephadex G-25 and carboxymethyl cellulose chromatography. Their purity was assessed by paper and thin layer chromatography, melting point, amino acid analysis and biological assay. The effect of blood pressure depression in rat by ($Try^8$) bradykinin was about 1.3 times as that of bradykinin, the standard. ($Tyr^5$), ($Tyr^8$), ($Tyr^5$, $Tyr^8$) and ($Trp^8$) analogues of bradykinin were incubated in vitro with endopeptidase ($alpha$-chymotrypsin) and exopeptidase (carboxypeptidase A, leucine aminopeptidase) in order to study the degradation patterns of peptides. Four bradykinin analogues were rapidly degradated by $alpha$-Chymotrypsin and carboxypeptidase A, while the degradation by leucine aminopeptidase is slow.