The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion

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. tes...

Full description

Bibliographic Details
Main Author: Low, Weini
Format: Project Paper Report
Language:English
Published: 2015
Online Access:http://psasir.upm.edu.my/id/eprint/78230/1/FBSB%202015%2059%20-%20IR.pdf
_version_ 1796980446483972096
author Low, Weini
author_facet Low, Weini
author_sort Low, Weini
collection UPM
description 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.
first_indexed 2024-03-06T10:23:08Z
format Project Paper Report
id upm.eprints-78230
institution Universiti Putra Malaysia
language English
last_indexed 2024-03-06T10:23:08Z
publishDate 2015
record_format dspace
spelling upm.eprints-782302020-06-26T02:34:03Z http://psasir.upm.edu.my/id/eprint/78230/ The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion Low, Weini 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. 2015-06 Project Paper Report NonPeerReviewed text en http://psasir.upm.edu.my/id/eprint/78230/1/FBSB%202015%2059%20-%20IR.pdf Low, Weini (2015) The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion. [Project Paper Report]
spellingShingle Low, Weini
The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion
title The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion
title_full The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion
title_fullStr The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion
title_full_unstemmed The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion
title_short The assessment of cholinesterase from gills of Anabus testudineus as detection of metal ion
title_sort assessment of cholinesterase from gills of anabus testudineus as detection of metal ion
url http://psasir.upm.edu.my/id/eprint/78230/1/FBSB%202015%2059%20-%20IR.pdf
work_keys_str_mv AT lowweini theassessmentofcholinesterasefromgillsofanabustestudineusasdetectionofmetalion
AT lowweini assessmentofcholinesterasefromgillsofanabustestudineusasdetectionofmetalion