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Título: | Phosphotriesterase activity identified in purified serum albumins |
Autor: | Sogorb, Miguel A.; Díaz-Alejo, Nuria CSIC; Escudero, María A. CSIC; Vilanova, Eugenio | Fecha de publicación: | 1998 | Editor: | Springer Nature | Citación: | Archives of Toxicology 72: 219-226 (1998) | Resumen: | The phosphotriesterase in chicken serum that hydrolyses O-hexyl O-2,5-dichlorophenyl phosphoramidate (HDCP) was purified in three chromatographic steps. The activity copurified to apparent homogeneity with albumin monitoring by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS/ PAGE) and by SDS-capillary electrophoresis in the purified fractions. Commercial chicken serum albumin was further purified and the phosphotriesterase activity remained associated with albumin. Capillary electrophoresis established a molecular weight of 59 +/- 4 kDa for both purified proteins (chicken serum and commercial chicken serum albumin). The purified samples were assayed for hydrolytic activity against several carboxylesters, organophosphates and phosphoramidates. From carboxylesters, only p-nitrophenylbutyrate (p-NPB) hydrolysing activity was found to copurify with the phosphotriesterase. The purified human, chicken, rabbit and bovine serum albumins and recombinant human serum albumin obtained from commercial sources hydrolysed HDCP and p-NPB. Serum albumin also hydrolysed O-butyl O-2,5-dichlorophenyl phosphoramidate, O-ethyl O-2,5-dichlorophenyl phosphoramidate and O-2,5-dichlorophenyl ethylphosphonoamidate but not other organophosphates and phosphoramidates. | Versión del editor: | https://doi.org/10.1007/s002040050492 | URI: | http://hdl.handle.net/10261/310249 | DOI: | 10.1007/s002040050492 | ISSN: | 0340-5761 |
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