RESUMO

Aprotinin, the most studied serine proteinase inhibitor, was isolated from porcine lung for the first time. The purified porcine aprotinin had an Mr value of ¡­7 kDa. It cross-reacted with polyclonal serum anti-commercial aprotinin. About 1 ¥ìg porcine aprotinin inhibited 6 ¥ìg trypsin whereas 1 ¥ìg commercial soybean inhibitor inhibited only 1 ¥ìg trypsin. The aprotinin gene was also isolated from porcine lung: the deduced amino acid sequence showed 74% identity to bovine aprotinin.

Assuntos

Masculino , Feminino , Animais , Aprotinina/isolamento & purificação , Suínos