고상법으로 개량된 기구에 의하여 bradykinin, $(Leu^1)$, $(Leu^2)$ 및 ($Ala^1$, $Ala^9$) bradykinin을 합성하였으며 이들 peptide의 정제 및 순도 측정에는 gel chromatography, paper chromatography, thin layer chromatography, paper electrophoresis, disc electrophoresis 및 아미노산 분석에 의거하였다. Endopeptidase인 ${alpha}$-chymotrypsin과 trypsin, exopeptidase인 carboxypeptidase A와 leucine aminopeptidase를 사용하여 in vitro 상에서 이들 peptide의 분해 실험을 됐다. ${alpha}$-Chymotrypsin과 carboxypeptidase는 peptide를 빠르게 분해하였으나 trypsin의 분해 작용은 느린 것으로 나타났다. Bradykinin, $(Leu^1)$과 ($Ala^1$, $Ala^9$) bradykinin에 는 N-말단에 모두 proline의 immino기와 결합되어 있기 때문에 leucine aminopeptidase의 작용을 받지 않았다.
Synthesis of bradykinin, $(Leu^1)$, $(Leu^2)$ and ($Ala^1$, $Ala^9$) analogues of bradykinin by solid phase method using an improved reaction vessel was carried out. We employed gel chromatography, paper chromatography, thin layer chromatography, paper electrophoresis, disc electrophoresis and amino acid analysis for purification and for determining the purity of synthesized peptides. Bradykinin, $(Leu^1)$, $(Leu^2)$ and ($Ala^1$, $Ala^9$) analogues of bradykinin were incubated in vitro with endopeptidases (${alpha}$-chymotrypsin, trypsin) and exopeptidase (carboxypeptidase A, leucine aminopeptidase) in girder to study the degradation patterns of the peptides. Eradykinin and $(Leu^1)$, $(Leu^2)$ and ($Ala^1$, $Ala^9$) analogues of bradykinin were rapidly degradated by ${alpha}$-chymotrypsin and carboxypeptidase A, while the degradation by trypsin is slow. Bradykinin, $(Leu^1)$ and ($Ala^1$, $Ala^9$) analogues of bradykinin contain immino peptide bond from proline at N-terminal and therefore they were not attacked by leucine aminopeptidase.
