Met-Lys-Bradykinin-Ser, the kinin released from human kininogen by human pepsin
- 作者：Gomes Silva ; Roseli A. ; Chagas ; Jair R. ; Juliano ; Luí ; s ; Hial ; Valdemar
- 关键词：Human pepsin ; Fluorogenic substrates ; Met-lys-bradykinin ; Met-lys-bradykinin-ser ; Kinin
- 刊名：Immunopharmacology
- 出版年：1996
- 期刊代码：43_01623109
- 类别：imm
- 出版时间：May, 1996
- 卷：32
- 期：1-3
- 页码：76-79
- 文件大小：176 K
摘要
This study was carried out to show the site in kininogen, using synthetic substrates, that is cleaved by a purified human pepsin component with a molecular weight of 35 000 daltons. The study used 4 (four) intramolecularly quenched fluorogenic substrates containing N- and C-terminal sequences around the methionyl-lysyl-bradykinin (MLBK) region of kininogen: Abz-LMKRP-Eddnp, Abz-MISLMKRP-Eddnp, Abz-FRSSR-Eddnp and Abz-RPPGFSPFRSSRQ-Eddnp. The hydrolysis on N-terminal sequences Abz-LMKRP-Eddnp and Abz-MISLMKRP-Eddnp occurred at L-M linkage and on C-terminal sequences Abz-FRSSR-Eddnp, and Abz-RPPGFSPFRSSRQ-Eddnp occurred at S-S linkage. The released peptide Abz-RPPGFSPFRS was able to contract rat uterus muscle. The results suggest that Met-Lys-Bradykinin-Ser, should be the peptide released from human kininogen by a purified human pepsin component.