| Summary: | Cholinesterase from the gill of Anabus testudineus contains mostly AChE. It was
partially purified by ammonium sulphate precipitation and DEAE cellulose using ion exchange
chromatography with 4.890U of specific activity, 11.7 of purification fold and 3.0%
yield. Optimum pH for AChE in gill of A. testudineus is 8 using Tris-HCl buffer at
temperature 25°C. The optimum acetylthiocholine iodide concentration is 2.5 mM with Vmₐₓ
2.533 and Km 0.8802 in which the catalytic efficiency of 2.88. For metal ion inhibition, 10
metal ions were tested and AChE in gill of Anabus testudineus showed a critically low
enzyme activity towards mercury in which the activity is inhibited by 99.05%. However,
cobalt and silver had no inhibitory effect on AChE. From IC₅₀, only 0.0123 ppm of Hg
was required to reduce the enzyme activity by half.
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