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Type: Artigo de periódico
Title: Purification And Characterization Of A Phosphodiesterase From Bothrops Alternatus Snake Venom.
Author: Valério, A A
Corradini, A C
Panunto, P C
Mello, S M
Hyslop, S
Abstract: A phosphodiesterase was purified from the venom of the snake Bothrops alternatus by a combination of gel filtration and ion exchange chromatographies. In SDS-PAGE, the enzyme gave a single band with a molecular mass of 105 kDa, which was unaltered in the presence of beta-mercaptoethanol, indicating that the protein contained no subunits. A single protein band was also observed in native PAGE. There were no contaminating 5'-nucleotidase, alkaline phosphatase and protease activities. The enzyme was recognized by commercial bothropic antiserum and gave a single band in immunoblotting. The enzyme had a pH optimum in the range of 7.5-9.5 and the optimum temperature was 60 degrees C, with activity being rapidly lost within 1 min at > or = 70 degrees C. The Km of the enzyme was 2.69 mM. PDE activity was potentiated by cobalt and, to a lesser extent, by calcium, whereas copper, manganese, zinc, EDTA, and beta-mercaptoethanol were inhibitory. These properties show that this enzyme is very similar to that isolated from other snake venoms.
Subject: Animals
Chromatography, Gel
Chromatography, Ion Exchange
Edetic Acid
Electrophoresis, Polyacrylamide Gel
Hydrogen-ion Concentration
Phosphoric Diester Hydrolases
Time Factors
Citation: Journal Of Protein Chemistry. v. 21, n. 8, p. 495-503, 2002-Nov.
Rights: fechado
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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