title: Characterization of the snake venoms from seven Brazilian species of Bothrops by FPLC anion-exchange chromatography.
abstract: 1. The elution profiles and the caseinolytic, myotoxic, coagulant and hemorrhagic activities of the venoms of seven Bothrops species fractionated on a Mono-Q FPLC column were analyzed. 2. Each venom separated into 16-20 peaks, with good reproducibility and the activities were concentrated in virtually discrete regions of the chromatogram. 3. There is a considerable overlap of active proteins in the different species venoms and our results indicate that a venom pool with the species B. jararaca, B. jararacussu, B. moojeni, B. neuwiedi and B. atrox venoms would contain the major active proteins determined in the seven species.
authors.affiliation: Biotechnology Center, Instituto Butantan, São Paulo, Brazil.
authors.forename: L C
authors.initials: LC
authors.lastname: Leite
authors.forename: M F
authors.initials: MF
authors.lastname: Furtado
authors.forename: T C
authors.initials: TC
authors.lastname: Correa
authors.forename: I
authors.initials: I
authors.lastname: Raw
mesh_terms: D000818:Animals; D001938:Brazil; D002364:Caseins; D002852:Chromatography, Ion Exchange; D003435:Crotalid Venoms / Q000737:chemistry* / Q000276:immunology / Q000633:toxicity; D006470:Hemorrhage / Q000139:chemically induced; D051379:Mice; D009132:Muscles / Q000187:drug effects; D010447:Peptide Hydrolases / Q000302:isolation & purification; D011506:Proteins / Q000302:isolation & purification; D012911:Snakes; D013045:Species Specificity; D013917:Thrombin / Q000302:isolation & purification
chemical_list: D002364:Caseins; D003435:Crotalid Venoms; D011506:Proteins; D010447:Peptide Hydrolases; D013917:Thrombin