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Doctoral Thesis
DOI
https://doi.org/10.11606/T.87.2008.tde-26062009-105405
Document
Author
Full name
Sandra de Cássia Dias
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 2008
Supervisor
Committee
Kubrusly, Flavia Saldanha (President)
Lebrun, Ivo
Polakiewicz, Bronislaw
Precioso, Alexander Roberto
Spencer, Patrick Jack
Title in Portuguese
Purificação e caracterização da aprotinina obtida de pulmão suíno.
Keywords in Portuguese
Circulação extracorpórea
Inibidores de enzimas
Proteínas
Proteinases
Suínos
Abstract in Portuguese
A aprotinina, um inibidor de serinoproteinase ácido resistente de massa molar de 7 kDa, é utilizada como insumo ou medicamento. O objetivo principal deste trabalho foi purificar a aprotinina a partir de pulmão suíno. Três procedimentos foram utilizados. O primeiro procedimento utilizou a coluna de tripsina-agarose, o segundo procedimento utilizou a filtração tangencial e coluna de tripsina-Sepharose. O terceiro procedimento utilizou três cromatografias: filtração em gel, troca-iônica e afinidade (tripsina-agarose). A aprotinina suína foi purificada de pulmão utilizando o terceiro procedimento. A seqüência parcial do gene da aprotinina suína apresentou 74% de identidade com a seqüência do gene da aprotinina bovina. Outros dois inibidores de serinoproteinases ácido resistentes foram purificados, são eles: o fragmento ativo do segundo domínio do inibidor de leucoprotease secretada (SLPI), e um segundo inibidor de alta massa molecular, provavelmente bikunina. O protocolo de purificação utilizado neste trabalho recuperou 85mg de aprotinina suína por kg de pulmão.
Title in English
Purification and characterization of the aprotinin from porcine lung.
Keywords in English
Extracorporeal circulation
Inhibitors of enzymes
Porcine
Proteinases
Proteins
Abstract in English
Aprotinin, an acid stable serine proteinase inhibitor with a molecular mass of 7 kDa, is used as a reagent or drug. The purification of the aprotinin from porcine lungs was the main objective of this work. Three procedures were used. The first one utilized the trypsin-agarose column. The tangential ultra filtration and trypsin-Sepharose column were used in the second procedure. And finally, the gel filtration, ion-exchange and affinity chromatography were employed in the third procedure. The porcine lung aprotinin was purified using the third procedure. The partial sequence of the aprotinin gene was obtained and showed 74% of the identity with the aprotinin bovine gene sequence. Another two acid stable serine proteinase inhibitors were purified: the active fragment of the secretory leukoprotease inhibitor second domain, and one high molecular mass inhibitor, probably bikunina. The purification protocol used in this work recovered 85mg of the porcine aprotinin from kg of lung.
 
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Publishing Date
2009-06-26
 
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