Purification And Partial Characterization Of A Thrombin-like Enzyme, Balterobin, From The Venom Of Bothrops Alternatus.

dc.creatorSmolka, M B
dc.creatorMarangoni, S
dc.creatorOliveira, B
dc.creatorNovello, J C
dc.date1998-Jul
dc.date2015-11-27T12:19:17Z
dc.date2015-11-27T12:19:17Z
dc.date.accessioned2018-03-29T00:52:53Z
dc.date.available2018-03-29T00:52:53Z
dc.identifierToxicon : Official Journal Of The International Society On Toxinology. v. 36, n. 7, p. 1059-63, 1998-Jul.
dc.identifier0041-0101
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/9690798
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194200
dc.identifier9690798
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294433
dc.descriptionA thrombin-like enzyme, balterobin, was purified from the venom of Bothrops alternatus. The purification steps included Sephadex G-75, heparin-sepharose and reverse phase HPLC C-18 column. Balterobin showed an apparent molecular weight of 30,000 in non-reduced conditions and displays a specific coagulant activity of 32.8 NIH units/mg over bovine fibrinogen. It also exhibits arginine amidase activity on DL-BAPNA. Like thrombin-like enzymes from other snakes, balterobin possesses valine as N-terminal residue, and is inhibited by PMSF.
dc.description36
dc.description1059-63
dc.languageeng
dc.relationToxicon : Official Journal Of The International Society On Toxinology
dc.relationToxicon
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAnimals
dc.subjectBothrops
dc.subjectCoagulants
dc.subjectCrotalid Venoms
dc.subjectFibrinogen
dc.subjectMolecular Weight
dc.subjectThrombin
dc.titlePurification And Partial Characterization Of A Thrombin-like Enzyme, Balterobin, From The Venom Of Bothrops Alternatus.
dc.typeArtículos de revistas


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