Isolation and preliminary enzymatic characterization of a novel PLA(2) from Crotalus durissus collilineatus venom

dc.creatorPonce-Soto, LA
dc.creatorToyama, MH
dc.creatorHyslop, S
dc.creatorNovello, JC
dc.creatorMarangoni, S
dc.date2002
dc.dateMAR
dc.date2014-11-17T11:16:12Z
dc.date2015-11-26T16:42:28Z
dc.date2014-11-17T11:16:12Z
dc.date2015-11-26T16:42:28Z
dc.date.accessioned2018-03-28T23:27:02Z
dc.date.available2018-03-28T23:27:02Z
dc.identifierJournal Of Protein Chemistry. Kluwer Academic/plenum Publ, v. 21, n. 3, n. 131, n. 136, 2002.
dc.identifier0277-8033
dc.identifierWOS:000175421100001
dc.identifier10.1023/A:1015332314389
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60842
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/60842
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60842
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1273264
dc.descriptionA crotoxin homolog was purified from the Crotalus durissus collilineatus venom using molecular exclusion and reverse-phase HPLC. This crotoxin contained one PLA(2) (Cdcolli III F6) and four crotapotin isoforms, whereas crotoxin from Crotalus durissus terrificus venom had three PLA(2) isoforms and two crotapotin isoforms. SDS-PAGE showed that the C. d. collilineatus PLA(2) and crotapotin had relative molecular mass of 15 and 9 kDa, respectively. Neither the PLA(2) (Cdcolli III F6) nor the crotapotins (Cdcolli III F3 and F4) had any neurotoxicity in mouse phrenic nerve-diaphragm preparations when tested alone. However, when PLA(2) and crotapotin were coincubated before testing, the neurotoxicity was restored to a level similar to test in the venom in native crotoxin. The two crotapotins (Cdcolli III F3 and F4) differed in their ability to inhibit PLA(2) activity, perhaps because of variations in their affinities for this enzyme. Cdcolli III F6 showed allosteric enzymatic behavior, with maximal activity at pH 8.3 and 36degreesC. Full PLA(2) activity required the presence of a low Ca2+ concentration and was inhibited by Cu2+ and Zn2+ and by Cu2+ and Mg2+ in the presence and absence of Ca2+, respectively. These results indicate that crotoxin from C. d. collineatus venom is very similar enzymatically to crotoxin from C. d. terrificus.
dc.description21
dc.description3
dc.description131
dc.description136
dc.languageen
dc.publisherKluwer Academic/plenum Publ
dc.publisherNew York
dc.publisherEUA
dc.relationJournal Of Protein Chemistry
dc.relationJ. Protein Chem.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectCrotalus durissus collilineatus
dc.subjectcrotapotin
dc.subjectcrotoxin
dc.subjectphospholipase A(2)
dc.subjectrattlesnake
dc.subjectvenom
dc.subjectPhospholipase A(2)
dc.subjectSnake-venom
dc.subjectCrotoxin Complex
dc.subjectTerrificus
dc.subjectIsoforms
dc.subjectMyotoxins
dc.subjectAssay
dc.titleIsolation and preliminary enzymatic characterization of a novel PLA(2) from Crotalus durissus collilineatus venom
dc.typeArtículos de revistas


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