Purification and characterization of aprotinin from porcine lungs
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
20/10/2012
20/10/2012
2008
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Resumo |
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 similar to 7 kDa. It cross- reacted with polyclonal serum anti- commercial aprotinin. About 1 mu g porcine aprotinin inhibited 6 mu g trypsin whereas 1 mu g commercial soybean inhibitor inhibited only 1 mu g trypsin. The aprotinin gene was also isolated from porcine lung: the deduced amino acid sequence showed 74% identity to bovine aprotinin. |
Identificador |
BIOTECHNOLOGY LETTERS, v.30, n.5, p.807-812, 2008 0141-5492 http://producao.usp.br/handle/BDPI/32190 10.1007/s10529-007-9622-0 |
Idioma(s) |
eng |
Publicador |
SPRINGER |
Relação |
Biotechnology Letters |
Direitos |
restrictedAccess Copyright SPRINGER |
Palavras-Chave | #aprotinin #BPTI #Kallikrein inactivator #Kunitz inhibitor #porcine aprotinin #porcine lungs #KALLIKREIN INHIBITOR #PROTEIN INHIBITORS #SURFACTANT #EVOLUTION #SYSTEM #Biotechnology & Applied Microbiology |
Tipo |
article original article publishedVersion |