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Type: Artigo de periódico
Title: Lmrtx, A Basic Pla₂ (d49) Purified From Lachesis Muta Rhombeata Snake Venom With Enzymatic-related Antithrombotic And Anticoagulant Activity.
Author: Damico, Daniela C S
Vassequi-Silva, T
Torres-Huaco, F D
Nery-Diez, A C C
de Souza, R C G
Da Silva, S L
Vicente, C P
Mendes, C B
Antunes, E
Werneck, C C
Marangoni, Sérgio
Abstract: A basic phospholipase A₂ (LmrTX) isoform was isolated from Lachesis muta rhombeata 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-5 Discovery® Bio Wide column. From liquid chromatography-electrospray ionization/mass spectrometry, the molecular mass of LmrTX was measured as 14.277.50 Da. The amino acid sequence showed a high degree of homology between PLA₂ LmrTX from L. muta rhombeata and other PLA₂ from snake venoms, like CB1 and CB2 from Crotalus durissus terrificus; LmTX-I and LmTX-II from Lachesis muta muta. LmrTX had PLA₂ activity in the presence of a synthetic substrate and alkylation of histidine residues significantly inhibited (P < 0.05) the enzymatic activity of LmrTX and its anticoagulant and antithrombotic activity. In this study, we examined the ability of the LmrTX in altering thrombus formation in living mouse, using a photochemically induced arterial thrombosis model. The control animals that did not receive protein injection showed a normal occlusion time, which was around 57 ± 7.8 min. LmrTX, the PLA₂ from L. muta rhombeata venom, caused a change in the occlusion time to 99 ± 10 min with doses of 7.5 μg/mice. Additionally, LmrTX showed the anticoagulant activity in vitro and ex vivo and prolonging the time aggregation in wash platelet induced by ADP and Thrombin.
Subject: Amino Acid Sequence
Base Sequence
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Liquid
Crotalid Venoms
Mass Spectrometry
Molecular Sequence Data
Phospholipases A2
Sequence Analysis, Dna
Species Specificity
Citation: Toxicon : Official Journal Of The International Society On Toxinology. v. 60, n. 5, p. 773-81, 2012-Oct.
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2012.06.010
Date Issue: 2012
Appears in Collections:Unicamp - Artigos e Outros Documentos

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