Artículos de revistas
Purification and characterization of aprotinin from porcine lungs
Fecha
2008Registro en:
BIOTECHNOLOGY LETTERS, v.30, n.5, p.807-812, 2008
0141-5492
10.1007/s10529-007-9622-0
Autor
DIAS, Sandra de Cassia
SAKAUCHI, Dirce
ABREU, Patricia Antonia Estima
LIMA NETTO, Solange de
IOURTOV, Dmitri
RAW, Isaias
KUBRUSLY, Flavia Saldanha
Institución
Resumen
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 similar to 7 kDa. It cross- reacted with polyclonal serum anti- commercial aprotinin. About 1 mu g porcine aprotinin inhibited 6 mu g trypsin whereas 1 mu g commercial soybean inhibitor inhibited only 1 mu g trypsin. The aprotinin gene was also isolated from porcine lung: the deduced amino acid sequence showed 74% identity to bovine aprotinin.