Biochemical and enzymatic characterization of two basic Asp(49) phospholipase A(2) isoforms from Lachesis muta muta (Surucucu) venom

dc.creatorDamico, DCS
dc.creatorLilla, S
dc.creatorde Nucci, G
dc.creatorPonce-Soto, LA
dc.creatorWinck, FV
dc.creatorNovello, JC
dc.creatorMarangoni, S
dc.date2005
dc.dateOCT 30
dc.date2014-11-15T04:34:54Z
dc.date2015-11-26T16:30:49Z
dc.date2014-11-15T04:34:54Z
dc.date2015-11-26T16:30:49Z
dc.date.accessioned2018-03-28T23:11:53Z
dc.date.available2018-03-28T23:11:53Z
dc.identifierBiochimica Et Biophysica Acta-general Subjects. Elsevier Science Bv, v. 1726, n. 1, n. 75, n. 86, 2005.
dc.identifier0304-4165
dc.identifier1872-8006
dc.identifierWOS:000233156800010
dc.identifier10.1016/j.bbagen.2005.05.022
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/55508
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/55508
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/55508
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1270059
dc.descriptionTwo basic phospholipase A(2) (PLA(2)) isoforms were isolated from Lachesis muta muta snake venom and partially characterized. The venom was fractionated by molecular exclusion chromatography in ammonium bicarbonate buffer followed by reverse-phase HPLC on a C-18 mu-Bondapack column and RP-HPLC on a C-8 column. From liquid chromatography-electrospray ionization/mass spectrometry, the molecular mass of the two isoforms LmTX-I and LmTX-II was respectively measured as 14,245.4 and 14,186.2 Da. The pI was respectively estimated to be 8.7 and 8.6 for LmTX-l and LmTX-II, as determined by two-dimensional electrophoresis. The two proteins were sequenced and differentiated from each other by a single amino acid substitution, Arg(65) (LmTX-I) -> Pro(65) (LmTX-II). The amino acid sequence showed a high degree of homology between PLA(2) isoforms from Lachesis muta muta and other PLA(2) snake venoms. LmTX-l and LmTX-II had PLA(2) activity in the presence of a synthetic substrate and showed a minimum sigmoidal behaviour; with maximal activity at pH 8.0 and 35-45 degrees C. Full PLA(2) activity required Ca2+ and was respectively inhibited by Cu2+ and Zn2+ in the presence and absence of Ca2+. Crotapotin from Crotalus durissus cascavella rattlesnake venom significantly inhibited (P < 0.05) the enzymatic activity of LmTX-I, suggesting that the binding site for crotapotin in this PLA(2) was similar to another in the basic PLA2 of the crotoxin complex from C. durissus cascavella venom. (c) 2005 Elsevier B.V. All rights reserved.
dc.description1726
dc.description1
dc.description75
dc.description86
dc.languageen
dc.publisherElsevier Science Bv
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationBiochimica Et Biophysica Acta-general Subjects
dc.relationBiochim. Biophys. Acta-Gen. Subj.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectcharacterization
dc.subjectenzyme
dc.subjectLachesis muta muta
dc.subjectphospholipase A(2)
dc.subjectsnake venom
dc.subjectCrotalus-durissus-terrificus
dc.subjectCrotoxin Complex
dc.subjectSnake-venom
dc.subjectMechanism
dc.subjectPurification
dc.subjectProtein
dc.subjectPla(2)
dc.subjectLoop
dc.titleBiochemical and enzymatic characterization of two basic Asp(49) phospholipase A(2) isoforms from Lachesis muta muta (Surucucu) venom
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución