Purification and characterization of aprotinin from porcine lungs.
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 approximately 7 kDa. It cross-reacted with polyclonal serum anti-commercial aprotinin. About 1 microg porcine aprotinin inhibited 6 microg trypsin whereas 1 microg commercial soybean inhibitor inhibited only 1 microg trypsin. The aprotinin gene was also isolated from porcine lung: the deduced amino acid sequence showed 74% identity to bovine aprotinin.
de Cássia Dias
Sandra
S
Centro de Biotecnologia, Avenida Vital Brasil, 1500, 05503-900, Sao Paulo, SP, Brazil.
Sakauchi
Dirce
D
Abreu
Patrícia Antonia Estima
PA
de Lima Netto
Solange
S
Iourtov
Dmitri
D
Raw
Isaias
I
Kubrusly
Flávia Saldanha
FS
D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000235:genetics* / Q000302:isolation & purification* / Q000378:metabolism; D001483:Base Sequence; D002417:Cattle; D002846:Chromatography, Affinity; D004247:DNA / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D008168:Lung / Q000378:metabolism*; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D013552:Swine; D014357:Trypsin / Q000378:metabolism
D004247:DNA; D007611:Aprotinin; D014357:Trypsin