Biochemical And Enzymatic Characterization Of Two Basic Asp49 Phospholipase A2 Isoforms From Lachesis Muta Muta (surucucu) Venom

dc.creatorDamico D.C.S.
dc.creatorLilla S.
dc.creatorDe Nucci G.
dc.creatorPonce-Soto L.A.
dc.creatorWinck F.V.
dc.creatorNovello J.C.
dc.creatorMarangoni S.
dc.date2005
dc.date2015-06-26T14:07:29Z
dc.date2015-11-26T15:41:46Z
dc.date2015-06-26T14:07:29Z
dc.date2015-11-26T15:41:46Z
dc.date.accessioned2018-03-28T22:50:19Z
dc.date.available2018-03-28T22:50:19Z
dc.identifier
dc.identifierBiochimica Et Biophysica Acta - General Subjects. , v. 1726, n. 1, p. 75 - 86, 2005.
dc.identifier3044165
dc.identifier10.1016/j.bbagen.2005.05.022
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-27144470280&partnerID=40&md5=3445883ff167c268e1dcaa2be6024ee0
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/93364
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/93364
dc.identifier2-s2.0-27144470280
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1264698
dc.descriptionTwo basic phospholipase A2 (PLA2) 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 μ-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-I 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) → Pro65 (LmTX-II). The amino acid sequence showed a high degree of homology between PLA2 isoforms from Lachesis muta muta and other PLA2 snake venoms. LmTX-I and LmTX-II had PLA2 activity in the presence of a synthetic substrate and showed a minimum sigmoidal behaviour; with maximal activity at pH 8.0 and 35-45°C. Full PLA2 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 PLA2 was similar to another in the basic PLA2 of the crotoxin complex from C. durissus cascavella venom. © 2005 Elsevier B.V. All rights reserved.
dc.description1726
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dc.description75
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dc.languageen
dc.publisher
dc.relationBiochimica et Biophysica Acta - General Subjects
dc.rightsfechado
dc.sourceScopus
dc.titleBiochemical And Enzymatic Characterization Of Two Basic Asp49 Phospholipase A2 Isoforms From Lachesis Muta Muta (surucucu) Venom
dc.typeArtículos de revistas


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