Cholinesterase from the common prawn (Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbarnate compounds

• Tipo: Artigo em Revista Científica Internacional
• Data: 2006

Autores

Manuela F Frasco (Autor) Outra; Didier Fournier (Autor) Outra; Felix Carvalho (Autor) FFUP; Ldcia Guilhermino (Autor) ICBAS

Revista

Título: Aquatic Toxicology

Vol. 77

Páginas: 412-421

ISSN: 0166-445X

Editora: Elsevier

Indexação

ISI Web of Knowledge - 41 Citações

Scopus - 45 Citações

Classificação Científica

FOS: Ciências médicas e da saúde > Medicina básica

Outras Informações

ID Authenticus: P-004-KQD

DOI: 10.1016/j.auqatox.2006.01.011

Abstract (EN): The main purpose of this study was to describe the kinetic properties of the cholinesterase (ChE) enzyme present in the eyes of the prawn Palaemon serratus, an abundant, ecological and commercially relevant species of European coastal environments. The obtained results suggest that the studied enzyme is a ChE and not a non-specific esterase, due to its apparent affinity for choline esters and the high sensitivity to eserine sulphate. This ChE displays a distinct preference for the substrate acetylthiocholine, showing a triphasic behaviour, with activation at low concentrations and inhibition by excess of substrate. Moreover, irreversible ChE inhibition by several organophosphate and carbamate compounds was characterized. All the irreversible inhibitions were homogeneous following a second-order rate reaction. The bimolecular rate constant (k(i)) values of ChE inhibition by the tested pesticides were also estimated and compared with available data from other invertebrate and vertebrate species. In conclusion, the results of the present study showed that prawn eyes possess only one ChE with typical properties of acetylcholinesterase, which is highly sensitive to the tested anti-cholinesterase compounds.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 10