Purification and characterization of aprotinin from porcine lungs

dc.creatorDIAS, Sandra de Cassia
dc.creatorSAKAUCHI, Dirce
dc.creatorABREU, Patricia Antonia Estima
dc.creatorLIMA NETTO, Solange de
dc.creatorIOURTOV, Dmitri
dc.creatorRAW, Isaias
dc.creatorKUBRUSLY, Flavia Saldanha
dc.date.accessioned2012-10-20T14:28:24Z
dc.date.accessioned2018-07-04T15:53:28Z
dc.date.available2012-10-20T14:28:24Z
dc.date.available2018-07-04T15:53:28Z
dc.date.created2012-10-20T14:28:24Z
dc.date.issued2008
dc.identifierBIOTECHNOLOGY LETTERS, v.30, n.5, p.807-812, 2008
dc.identifier0141-5492
dc.identifierhttp://producao.usp.br/handle/BDPI/32190
dc.identifier10.1007/s10529-007-9622-0
dc.identifierhttp://dx.doi.org/10.1007/s10529-007-9622-0
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1628823
dc.description.abstractAprotinin, 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.
dc.languageeng
dc.publisherSPRINGER
dc.relationBiotechnology Letters
dc.rightsCopyright SPRINGER
dc.rightsrestrictedAccess
dc.subjectaprotinin
dc.subjectBPTI
dc.subjectKallikrein inactivator
dc.subjectKunitz inhibitor
dc.subjectporcine aprotinin
dc.subjectporcine lungs
dc.titlePurification and characterization of aprotinin from porcine lungs
dc.typeArtículos de revistas


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