1.
Biotechnology Letters
; 30(5): 807-812, 2007.
Article
in English
| Sec. Est. Saúde SP, SESSP-IBPROD, Sec. Est. Saúde SP, SESSP-IBACERVO
| ID: biblio-1060892
ABSTRACT
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.
