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 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.
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Acknowledgments
The authors are in debt to Mr. Leo Setsuo Kobashi for his technical assistance. This work was supported by grants and scholarships from Brazilian agencies: CNPq, FAPESP, Capes/MEC and by Butantan Foundation and Sadia.
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de Cássia Dias, S., Sakauchi, D., Abreu, P.A.E. et al. Purification and characterization of aprotinin from porcine lungs. Biotechnol Lett 30, 807–812 (2008). https://doi.org/10.1007/s10529-007-9622-0
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DOI: https://doi.org/10.1007/s10529-007-9622-0