Purification and characterization of aprotinin from porcine lungs

• Published in: Biotechnology letters Vol. 30; no. 5; pp. 807 - 812
• Main Authors: de Cássia Dias, Sandra, Sakauchi, Dirce, Abreu, Patrícia Antonia Estima, de Lima Netto, Solange, Iourtov, Dmitri, Raw, Isaias, Kubrusly, Flávia Saldanha
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01-05-2008; Springer; Springer Nature B.V
• Subjects: Amino Acid Sequence; Amino acids; Animals; Applied Microbiology; Aprotinin - genetics; Aprotinin - isolation & purification; Aprotinin - metabolism; Base Sequence; Biochemistry; Biological and medical sciences; Biomedical and Life Sciences; Biotechnology; Cattle; Chromatography, Affinity; DNA - genetics; Electrophoresis, Polyacrylamide Gel; Enzymes; Fundamental and applied biological sciences. Psychology; Hogs; Life Sciences; Lung - metabolism; Lungs; Microbiology; Molecular Sequence Data; Original Research Paper; Polymerase Chain Reaction; Proteinase inhibitors; Sequence Homology, Amino Acid; Soybeans; Swine; Trypsin - metabolism; Kallikrein inactivator; Porcine aprotinin; Porcine lungs; Aprotinin; Kunitz inhibitor; BPTI; Purification; Lung; Pig; Aprotinin, BPTI; Characterization; Kallikrein inactivator,Kunitz inhibitor; Vertebrata; Mammalia; Porcine aprotinin,Porcine lungs; Inhibitor; Artiodactyla; Ungulata
• ISSN: 0141-5492; 1573-6776
• DOI: 10.1007/s10529-007-9622-0

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 μg porcine aprotinin inhibited 6 μg trypsin whereas 1 μg commercial soybean inhibitor inhibited only 1 μg trypsin. The aprotinin gene was also isolated from porcine lung: the deduced amino acid sequence showed 74% identity to bovine aprotinin.