Please use this identifier to cite or link to this item:
|Type:||Artigo de periódico|
|Title:||Purification from Bothrops lanceolatus (fer de lance) venom of a fibrino(geno)lytic enzyme with esterolytic activity|
|Author:||De Araujo, AL|
|Abstract:||Bothrops lanceolatus venom has high caseinolytic, phospholipasic, esterolytic and hemorrhagic activities. In spite of having no coagulant effect on plasma, this venom contains a thrombin-like enzyme. Using gel filtration and ion-exchange chromatographies, we have purified an esterolytic fraction (F-II-la) from this venom with a protein yield of 4% and a 58% recovery in enzyme activity. SDS-PAGE in the presence of beta-mercaptoethanol showed that the enzyme is a single chain polypeptide with a M-w = 38,100. Immunodiffusion and immunoelectrophoresis of fraction F-II-la against serum from horses immunized with B. lanceolatus venom and against rabbit antiserum prepared using fraction F-II-la both showed a single immunoprecipitin line. The K-m and V-max values for TAME hydrolysis were 0.85 mM and 38.6 mu mol/min/mg, respectively. The esterolytic activity was completely inhibited by PMSF (10 mM) but not by EDTA (20 mM). Fraction F-II-la hydrolyzed the alpha and beta chains of fibrinogen. Degradation of the a chain occurred within 10 min while that of the beta-chain was slower. The enzyme had no effect on the gamma-chain even after 4 h of hydrolysis. (C) 1998 Elsevier Science Ltd. All rights reserved.|
|Editor:||Pergamon-elsevier Science Ltd|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.