Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58471
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
Donato, JL
Bon, C
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.
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/S0041-0101(97)00118-9
Date Issue: 1998
Appears in Collections:Unicamp - Artigos e Outros Documentos

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