Characterization of acetylcholinesterase molecular forms of the root-knot nematode, Meloidogyne. Export

@article{citeulike:3290788, abstract = {Multiple molecular forms of acetylcholinesterase have been isolated and characterized from the root-knot nematodes Meloidogyne arenaria and Meloidogyne incognita. The forms of enzyme present in these 2 species are similar but not identical to those that occur in the free-living nematode Caenorhabditis elegans. The 5 enzyme forms exhibit differential solubilities and can be classified into 3 classes, A, B, and C, based on substrate affinity, inhibitor and detergent sensitivity, and thermal inactivation profiles. An unusual class of acetylcholinesterase has been isolated from Meloidogyne which has very high affinity for acetylcholine, but is highly resistant to carbamate and organophosphate inhibitors. The potential roles of the molecular forms in nematode behavior and sensitivity to nematicides are discussed.}, author = {Chang, S. H. and Opperman, C. H.}, citeulike-article-id = {3290788}, citeulike-linkout-0 = {http://www.wormbase.org/db/misc/paper?name=WBPaper00012277}, journal = {Molecular and Biochemical Parasitology}, keywords = {acetylcholinesterase\_classification, acetylcholinesterase\_metabolism, article, c\_elegans, caenorhabditis\_elegans, celegans, centrifugation\_density\_gradient, chromatography\_ion\_exchange, elegans, nematode, tylenchoidea\_enzymology, wormbase}, pages = {205--214}, posted-at = {2008-09-18 22:17:01}, priority = {3}, title = {Characterization of acetylcholinesterase molecular forms of the root-knot nematode, Meloidogyne.}, url = {http://www.wormbase.org/db/misc/paper?name=WBPaper00012277}, volume = {49}, year = {1991} }

TY - JOUR ID - citeulike:3290788 L3 - citeulike-article-id:3290788 N2 - Multiple molecular forms of acetylcholinesterase have been isolated and characterized from the root-knot nematodes Meloidogyne arenaria and Meloidogyne incognita. The forms of enzyme present in these 2 species are similar but not identical to those that occur in the free-living nematode Caenorhabditis elegans. The 5 enzyme forms exhibit differential solubilities and can be classified into 3 classes, A, B, and C, based on substrate affinity, inhibitor and detergent sensitivity, and thermal inactivation profiles. An unusual class of acetylcholinesterase has been isolated from Meloidogyne which has very high affinity for acetylcholine, but is highly resistant to carbamate and organophosphate inhibitors. The potential roles of the molecular forms in nematode behavior and sensitivity to nematicides are discussed. JF - Molecular and Biochemical Parasitology EP - 214 TI - Characterization of acetylcholinesterase molecular forms of the root-knot nematode, Meloidogyne. VL - 49 SP - 205 KW - acetylcholinesterase_classification KW - acetylcholinesterase_metabolism KW - article KW - c_elegans KW - caenorhabditis_elegans KW - celegans KW - centrifugation_density_gradient KW - chromatography_ion_exchange KW - elegans KW - nematode KW - tylenchoidea_enzymology KW - wormbase AU - Chang, SH AU - Opperman, CH PY - 1991/// UR - http://www.wormbase.org/db/misc/paper?name=WBPaper00012277 ER -