Soluble form of acetylcholinesterase from rabbit enterocytes: comparison of its molecular properties with those of the plasma membrane species |
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| Authors: | J P Sine B Colas |
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| Affiliation: | 1. Scientific Services Unit, Capricorn District Municipality, 24 Thabo Mbeki Street, Polokwane, 0699, South Africa;2. Department of Environmental Sciences, University of South Africa, Christaan de Wet Road, Florida, 1709, South Africa;3. Onderstepoort Veterinary Research, Agricultural Research Council, 100 Old Soutpan Road, Onderstepoort, Pretoria, 0110, South Africa;4. Scientific Services, Rand Water, 2 Barrage Road, Vereeniging, 1930, South Africa;5. Department of Water, Environmental and Earth Sciences, Tshwane University of Technology, 75 Mandela Drive, Pretoria, 0001, South Africa;1. Department of Chemistry, Faculty of Science, Universiti Brunei Darussalam, Jalan Tungku Link, Gadong, Brunei Darussalam;2. Department of Biological Sciences, Faculty of Science, Universiti Brunei Darussalam, Jalan Tungku Link, Gadong, Brunei Darussalam;1. United States Department of Agriculture, Agricultural Research Service, Thad Cochran Southern Horticultural Laboratory, 810 Highway 26 West, Poplarville, MS, 39470, USA;2. Center for Integrated Fungal Research, Department of Entomology and Plant Pathology, Partners Building III 239, North Carolina State University, Raleigh, NC, 27695, USA;1. Department of Chemistry/Nanoscience, Kannur University, Swami AnandhaTheertha campus, Payyannur, Edat P.O., Kerala, 670 327, India;2. Centre for Nano and Material Sciences, Jain, Jain Global Campus, Bangalore, 52112, Karnataka, India;3. The Surface Analysis Laboratory, Department of Mechanical Engineering Sciences, University of Surrey, Guildford, Surrey, GU2 7XH, UK;4. Nanotechnology and Bio-Engineering Research Group, Department of Environmental Sciences, Institute of Technology Sligo, Ireland and Centre for Precision Engineering, Materials andManufacturing Research, Department of Environmental Science, Institute of Technology Sligo, Ash Lane, Sligo, Ireland |
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| Abstract: | ![]()
A soluble form of acetylcholinesterase was shown to be present in rabbit enterocytes. The enzyme was obtained from a high-speed supernatant (105,000 X g centrifugation) after homogenization of intestinal mucosa without detergent. It was shown to possess no obvious hydrophobic character and could be classified as a low-salt-soluble (LSS) acetylcholinesterase. Sucrose gradient centrifugation revealed a single enzyme species with a sedimentation coefficient of 3.9 +/- 0.2S. By gel filtration performed in HPLC the enzyme was eluted as a protein corresponding to an Mr of 72,000 +/- 3,000. It could be precipitated with concanavalin A by affinoelectrophoresis, but the catalytic activity was not affected by the lectin. Our results are consistent with a G1 globular form for this soluble acetylcholinesterase which differs very clearly from detergent-soluble forms also found recently in the plasma membranes of rabbit enterocytes. |
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