dc.creatorBonfim, VL
dc.creatorPonce-Soto, LA
dc.creatorNovello, JC
dc.creatorMarangoni, S
dc.date2006
dc.dateDEC
dc.date2014-11-19T22:30:47Z
dc.date2015-11-26T18:06:38Z
dc.date2014-11-19T22:30:47Z
dc.date2015-11-26T18:06:38Z
dc.date.accessioned2018-03-29T00:48:49Z
dc.date.available2018-03-29T00:48:49Z
dc.identifierProtein Journal. Springer, v. 25, n. 41858, n. 492, n. 502, 2006.
dc.identifier1572-3887
dc.identifierWOS:000242661500006
dc.identifier10.1007/s10930-006-9033-4
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/79650
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/79650
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/79650
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1293406
dc.descriptionCr 5 PLA(2) homologous (K49) was isolated from Calloselasma rhodostoma venom in only one chromatographic step in reverse phase HPLC (RP-HPLC) (on mu-Bondapack C-18). A molecular mass of 13.965 Da was determined by MALDI-TOF mass spectrometry. The amino acid composition showed that Cr 5 had a high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical residues of a basic PLA(2). The complete amino acid sequence of Cr 5 PLA(2) contains 120 residues, resulting in a calculated pI value of 5.55. This sequence shows high identity values when compared to other K49 PLA(2)s isolated from the venoms of viperid snakes. Lower identity is observed in comparison to D49 PLA(2)s. The sequence found was SLVELGKMIL QETGKNPAKS YGAYGCNCGV LGRHKPKDAT DRCCFVHKCC YKKLTGCDPK KDRYSYSWKD KTIVCGENNP CLKEMCECDK AVAICLRENL DTYNKKYRYL KPFCKKADDC. In mice, Cr 5 induced myonecrosis and edema upon intramuscular and intravenous injections, respectively. The LD50 of Cr 5 was 0.070 mg/kg of the animal weight, by intracerebroventricular (i.c.v.) route. In vitro, the toxin caused rapid cytolytic effect upon mouse skeletal muscle myoblasts in culture. The isolation of this PLA(2) and the combined structural and functional information obtained classify Cr 5 as a new member of the K49 PLA(2) family, since it presents typical features from such proteins.
dc.description25
dc.description41858
dc.description492
dc.description502
dc.languageen
dc.publisherSpringer
dc.publisherNew York
dc.publisherEUA
dc.relationProtein Journal
dc.relationProtein J.
dc.rightsfechado
dc.rightshttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.sourceWeb of Science
dc.subjectphospholipase A(2)
dc.subjectLys49
dc.subjectmyotoxin
dc.subjectsnake venom
dc.subjectCalloselasma rhodostoma
dc.subjectBothrops-alternatus
dc.subjectA(2) Enzymes
dc.subjectPiratoxin-ii
dc.subjectMyotoxin-ii
dc.subjectIn-vitro
dc.subjectAcid
dc.subjectMechanism
dc.subjectProteins
dc.subjectSequence
dc.subjectInsights
dc.titleStructural and functional properties of Cr 5, a new Lys49 phospholipase A(2) homologue isolated from the venom of the snake Calloselasma rhodostoma
dc.typeArtículos de revistas


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