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- Title
Characterization of acetylcholinesterase from the gut of sea cucumber Stichopus japonicus.
- Authors
Wu, Hai-Tao; Li, Dong-Mei; Zhu, Bei-Wei; Du, Ying; Chai, Xiao-Qian; Murata, Yoshiyuki
- Abstract
An acetylcholinesterase was purified from the gut of sea cucumber Stichopus japonicus by anion exchange chromatography followed by gel filtration chromatography. The enzyme was purified 35.49-fold with a total yield of 7.73 %. The molecular mass of purified acetylcholinesterase was 68 kDa as revealed on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme displayed maximum activity at pH 7.5 and 35 °C with acetylthiocholine iodide as substrate. The enzyme activity appeared to be stable over pH 6.0-8.0 and up to 40 °C. It displayed an apparent Michaelis-Menten behavior in the concentration range from 0.1 to 0.8 mM with K values of 0.62 mM for acetylthiocholine iodide and 2.53 mM for butyrylthiocholine iodide. More than 95 % of acetylcholinesterase activity was inhibited by 1 mM eserine or 1,5-bis(4-allyldimethylammonium phenyl)-pentan-3-one dibromide (BW284C51), but only 19.1 % of the activity was inhibited by tetraisopropylpyrophosphoramide (iso-OMPA) at the same concentration. On the basis of the substrate and inhibitor specificities, the purified enzyme appeared to be a true acetylcholinesterase. Nevertheless, the purified acetylcholinesterase exhibited insensitivity to substrate inhibition phenomenon. Its biochemical properties were compared with those reported for different species.
- Subjects
ACETYLCHOLINESTERASE; SEA cucumbers; APOSTICHOPUS japonicus; CHROMATOGRAPHIC analysis; GEL permeation chromatography
- Publication
Fisheries Science, 2013, Vol 79, Issue 2, p303
- ISSN
0919-9268
- Publication type
Article
- DOI
10.1007/s12562-012-0588-z