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http://purl.uniprot.org/citations/16626776http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16626776http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16626776http://www.w3.org/2000/01/rdf-schema#comment"The whole venom of Lachesis muta muta is preponderantly neurotoxic but moderately myotoxic on the chick biventer cervicis preparation (BCp). We have now examined these toxic activities of a basic phospholipase A(2), LmTX-I, isolated from the whole venom. LmTX-I caused a significant concentration-dependent neuromuscular blockade in the BCp. The time to produce 50% neuromuscular blockade was 14.7+/-0.75 min (30 microg/ml), 23.6+/-0.9 min (10 microg/ml), 34+/-1.7 min (2.5 microg/ml) and 39.2+/-3.6 min (1 microg/ml), (n=5/concentration; p<0.05). Complete blockade with all tested concentrations was not accompanied by inhibition of the response to ACh. At the highest concentration, LmTX-I (30 microg/ml) significantly reduced contractures elicited by exogenous KCl (20mM), increased the release of creatine kinase (1542.5+/-183.9 IU/L vs 442.7+/-39.8 IU/L for controls after 120 min, p<0.05), and induced the appearance of degenerating muscle fibers ( approximately 15%). Quantification of myonecrosis indicated 14.8+/-0.8 and 2.0+/-0.4%, with 30 and 10 microg/mlvenom concentration, respectively, against 1.07+/-0.4% for control preparations. The findings indicate that the basic PLA(2) present on venom from L. m. muta (LmTX-I) possesses a dominant neurotoxic action on isolated chick nerve-muscle preparations, whereas myotoxicity was mainly observed at the highest concentration used (30 microg/ml). These effects of LmTX-I closely reproduce the effects of the whole venom of L. m. muta in chick neuromuscular preparations."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.org/dc/terms/identifier"doi:10.1016/j.toxicon.2006.02.007"xsd:string
http://purl.uniprot.org/citations/16626776http://purl.org/dc/terms/identifier"doi:10.1016/j.toxicon.2006.02.007"xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Rodrigues-Simioni L."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Rodrigues-Simioni L."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Marangoni S."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Marangoni S."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Novello J.C."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Novello J.C."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Bueno L.G.F."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Bueno L.G.F."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Damico D.C.S."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"Damico D.C.S."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"da Cruz-Hofling M.A."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/author"da Cruz-Hofling M.A."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/name"Toxicon"xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/name"Toxicon"xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/pages"759-765"xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/pages"759-765"xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/title"Functional characterization of a basic D49 phospholipase A2 (LmTX-I) from the venom of the snake Lachesis muta muta (bushmaster)."xsd:string
http://purl.uniprot.org/citations/16626776http://purl.uniprot.org/core/title"Functional characterization of a basic D49 phospholipase A2 (LmTX-I) from the venom of the snake Lachesis muta muta (bushmaster)."xsd:string