A novel butyrylcholinesterase from serum of Leporinus macrocephalus, a Neotropical fish

We show here that serum of piaussu, a Neotropical characin fish, has the highest butyrylcholinesterase activity so far described for humans and fish. To clarify whether this cholinesterase could protect piaussu against anticholinesterase pesticides by scavenging organophosphates, we purified it 1700...

Full description

Saved in:
Bibliographic Details
Published in:Biochimie 2006, Vol.88 (1), p.59-68
Main Authors: Salles, J.B., Cunha Bastos, V.L.F., Silva Filho, M.V., Machado, O.L.T., Salles, C.M.C., Giovanni de Simone, S., Cunha Bastos, J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Butyrylcholinesterase
Butyrylcholinesterase - blood
Butyrylcholinesterase - isolation & purification
Butyrylcholinesterase - metabolism
Butyrylthiocholine - metabolism
Chlorpyrifos - analogs & derivatives
Chlorpyrifos - pharmacology
Cholinesterase Inhibitors - pharmacology
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Fish poisoning
Fishes - blood
Freshwater
Humans
Leporinus macrocephalus
Molecular Sequence Data
Organophosphate Poisoning
Organophosphorus
Paraoxon - analogs & derivatives
Paraoxon - pharmacology
Piaussu
Poisoning - prevention & control
Sequence Alignment
Tetraisopropylpyrophosphamide - pharmacology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:We show here that serum of piaussu, a Neotropical characin fish, has the highest butyrylcholinesterase activity so far described for humans and fish. To clarify whether this cholinesterase could protect piaussu against anticholinesterase pesticides by scavenging organophosphates, we purified it 1700-fold, with a yield of 80%. Augmenting concentrations (from 0.01 to 20 mM) of butyrylthiocholine activated it. The pure enzyme was highly inhibited by chlorpyriphos-oxon ( k i = 10,434 × 10 6 M −1 min −1) and by the specific butyrylcholinesterase inhibitor, isoOMPA ( k i = 45.7 × 10 6 M −1 min −1). Electrophoresis of total serum and 2-D electrophoresis of the purified cholinesterase showed that some enzyme molecules could circulate in piaussu serum as heterogeneously glycosylated dimers. The enzyme's N-terminal sequence was similar to sequences found for butyrylcholinesterase from sera of other vertebrates. Altogether, our data present a novel butyrylcholinesterase with the potential of protecting a fish from poisoning by organophosphates.
ISSN:0300-9084
1638-6183
DOI:10.1016/j.biochi.2005.06.017