dc.creatorLomonte, Bruno
dc.creatorGutiérrez, José María
dc.date.accessioned2016-11-07T19:45:42Z
dc.date.accessioned2022-10-19T23:36:18Z
dc.date.available2016-11-07T19:45:42Z
dc.date.available2022-10-19T23:36:18Z
dc.date.created2016-11-07T19:45:42Z
dc.date.issued1990
dc.identifierhttp://www.sciencedirect.com/science/article/pii/004101019090088O
dc.identifier0041-0101
dc.identifierhttps://hdl.handle.net/10669/29160
dc.identifierdoi:10.1016/0041-0101(90)90088-O
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4520427
dc.description.abstractIN A RECENT article KASTURi and GOWDA,(1990) described the dissociation of enzymatic and toxic activities of phospholipases A, (PLA) from Vipera russelli venom by neutraliza- tion experiments using rabbit polyclonal antibodies . The authors conclude that their results "have shown the presence of distinct sites on the same PLA 2 molecule responsible for neurotoxicity, catalytic activity, anticoagulant activity and myotoxicity" . Also they state that "there are no reports explaining the relationship between the catalytic activity and pharmacological properties making use of these (polyclonal) antibodies", and "For the first time we are reporting the presence of multiple pharmacological sites on the PLA 2 molecule apart from the catalytic site using polyclonal antibodies"
dc.languageen_US
dc.sourceToxicon 28(11):1245-7, 1990
dc.subjectAnimals
dc.subjectAntibodies
dc.subjectImmune Sera
dc.subjectPhospholipases A
dc.subjectVenoms
dc.subjectImmunology
dc.subjectSnake venom
dc.titleDissociation of enzymatic and toxic activities by the use of antibodies
dc.typeartículo científico


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