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dc.creatorLomonte, Bruno
dc.creatorKahan, Lawrence
dc.date.accessioned2017-08-08T21:51:47Z
dc.date.available2017-08-08T21:51:47Z
dc.date.issued1988
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/0041010188902498
dc.identifier.issn0041-0101
dc.identifier.urihttps://hdl.handle.net/10669/72949
dc.description.abstractSeven murine monoclonal antibodies against Bothrops aspen myotoxin were produced and partially characterized. They revealed the presence of at least four cross-reacting basic components in crude venom, with a common subunit mol. wt of 16,000 by sodium dodecylsulfate-polyacrylamide gel electrophoresis, but slight differences in charge. These myotoxin-related components might be isoforms of the toxin . By Western blotting and enzyme-immunoassay binding techniques, differences in the reactivities with basic venom fractions were observed among monoclonal antibodies, suggesting differences in epitope specifidties . Three antibodies cross-reacted with B. nummifer crude venom. Two monoclonal antibodies were utilized to develop a two-site enzyme-immunoassay for myotoxin detection at the nanogram level . Three of the antibodies (one IgM and two IgG,) showed ability to neutralize myotoxiclty of purified myotoxin in preincubation-type experiments.es_ES
dc.description.sponsorshipUniversity of Wisconsin/[08387]//Estados Unidoses_ES
dc.language.isoen_USes_ES
dc.sourceToxicon 26(7), 675-689 (1988)es_ES
dc.subjectanticuerposes_ES
dc.subjectmonoclonaleses_ES
dc.subjectmiotoxinaes_ES
dc.titleProduction and partial characterization of monoclonal antibodies to Bothrops asper (terciopelo) myotoxines_ES
dc.typeartículo original
dc.identifier.doi10.1016/0041-0101(88)90249-8
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid3140427


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