Purification and characterization of the aprotinin from porcine lung. / Purificação e caracterização da aprotinina obtida de pulmão suíno.

AUTOR(ES)

Sandra de Cássia Dias

DATA DE PUBLICAÇÃO

2008

RESUMO

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.

ASSUNTO(S)

inibidores de enzimas extracorporeal circulation porcine proteinases proteins circulação extracorpórea inhibitors of enzymes proteínas suínos proteinases

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