LmrTX, a basic PLA2 (D49) purified from Lachesis muta rhombeata snake venom with enzymatic-related antithrombotic and anticoagulant activity

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...

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Bibliographic Details
Published in:Toxicon (Oxford) 2012-10, Vol.60 (5), p.773-781
Main Authors: 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
Format: Article
Language:English
Subjects:
adenosine diphosphate
alkylation
Amino Acid Sequence
amino acid sequences
ammonium bicarbonate
Animal poisons toxicology. Antivenoms
Animals
Anticoagulant activity
anticoagulants
Arterial thrombosis
Base Sequence
Biological and medical sciences
Blood and lymphatic vessels
Cardiology. Vascular system
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Liquid
Crotalid Venoms - enzymology
Crotalus durissus terrificus
Diseases of the peripheral vessels. Diseases of the vena cava. Miscellaneous
enzyme activity
gel chromatography
histidine
ionization
Lachesis muta
Lachesis muta rhombeata venom
Mass Spectrometry
Medical sciences
Mice
Molecular Sequence Data
molecular weight
Phospholipase A2
Phospholipases A2 - genetics
Phospholipases A2 - metabolism
Photochemical injury
Platelet aggregation
reversed-phase high performance liquid chromatography
Sequence Analysis, DNA
snakes
Species Specificity
thrombin
thrombosis
Thrombosis - chemically induced
Toxicology
venoms
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Description
Summary: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 
ISSN:0041-0101
1879-3150
DOI:10.1016/j.toxicon.2012.06.010