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Purification and characterization of aprotinin from porcine lungs |
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| Authors: | Sandra de Cássia Dias Dirce Sakauchi Patrícia Antonia Estima Abreu Solange de Lima Netto Dmitri Iourtov Isaias Raw Flávia Saldanha Kubrusly |
| Institution: | Centro de Biotecnologia, Avenida Vital Brasil, 1500, 05503-900, Sao Paulo, SP, Brazil. |
| 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. |
| Keywords: | Aprotinin BPTI Kallikrein inactivator Kunitz inhibitor Porcine aprotinin Porcine lungs |
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