title: Purification and characterization of aprotinin from porcine lungs.
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 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.
authors: Centro de Biotecnologia, Avenida Vital Brasil, 1500, 05503-900, Sao Paulo, SP, Brazil.
authors: Sandra
authors: S
authors: de Cássia Dias
authors: Dirce
authors: D
authors: Sakauchi
authors: Patrícia Antonia Estima
authors: PA
authors: Abreu
authors: Solange
authors: S
authors: de Lima Netto
authors: Dmitri
authors: D
authors: Iourtov
authors: Isaias
authors: I
authors: Raw
authors: Flávia Saldanha
authors: FS
authors: Kubrusly
mesh_terms: 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
chemical_list: D004247:DNA; D007611:Aprotinin; D014357:Trypsin