Abstract
Phospholipases A2 (PLA2s) are enzymes responsible for inflammatory effects, edema formation, myotoxicity, neurotoxicity and other manifestations from envenoming. In this paper we report the isolation and biochemical characterization of Lmr-PLA2, the first acidic PLA2 found in Lachesis muta rhombeata venom. Furthermore, this study compared biological effects of Lmr-PLA2 and crotoxin B (CB), a PLA2 from Crotalus durissus terrificus venom. Lmr-PLA2 was isolated by molecular exclusion and reversed phase chromatography. The purified enzyme showed a molecular mass of 13,975 Da, pI of 5.46 and its partial amino acid sequence showed a high identity with PLA2s already described in the literature. In addition, this enzyme possesses the residue D49 in its amino acid sequence, indicating that it is a catalytically active PLA2. Lmr-PLA2 presented high phospholipase activity and was able to inhibit platelet aggregation. Studies of biochemical characterization of new PLA2s, as Lmr-PLA2, are relevant since they help to clarify the structure-function relationship of this important class of toxins.
Keywords: Acidic phospholipase A2, crotoxin B, edema, Lachesis muta rhombeata, myotoxicity, snake venom.
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Protein & Peptide Letters
Title:A New Phospholipase A2 from Lachesis muta rhombeata: Purification, Biochemical and Comparative Characterization with Crotoxin B
Volume: 22 Issue: 9
Author(s): Francielle A. Cordeiro, Tibério G.K. Perini, Cristiane Bregge-Silva, Caroline M. Cremonez, Renata S. Rodrigues, Johara Boldrini-França, Karla de C.F. Bordon, Dayane L.N. De Souza, David C. Ache, Veridiana de M. Rodrigues, Wagner F. dos Santos, Jose C. Rosa and Eliane C. Arantesa
Affiliation:
Keywords: Acidic phospholipase A2, crotoxin B, edema, Lachesis muta rhombeata, myotoxicity, snake venom.
Abstract: Phospholipases A2 (PLA2s) are enzymes responsible for inflammatory effects, edema formation, myotoxicity, neurotoxicity and other manifestations from envenoming. In this paper we report the isolation and biochemical characterization of Lmr-PLA2, the first acidic PLA2 found in Lachesis muta rhombeata venom. Furthermore, this study compared biological effects of Lmr-PLA2 and crotoxin B (CB), a PLA2 from Crotalus durissus terrificus venom. Lmr-PLA2 was isolated by molecular exclusion and reversed phase chromatography. The purified enzyme showed a molecular mass of 13,975 Da, pI of 5.46 and its partial amino acid sequence showed a high identity with PLA2s already described in the literature. In addition, this enzyme possesses the residue D49 in its amino acid sequence, indicating that it is a catalytically active PLA2. Lmr-PLA2 presented high phospholipase activity and was able to inhibit platelet aggregation. Studies of biochemical characterization of new PLA2s, as Lmr-PLA2, are relevant since they help to clarify the structure-function relationship of this important class of toxins.
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Cordeiro A. Francielle, Perini G.K. Tibério, Bregge-Silva Cristiane, Cremonez M. Caroline, Rodrigues S. Renata, Boldrini-França Johara, C.F. Bordon de Karla, De Souza L.N. Dayane, Ache C. David, M. Rodrigues de Veridiana, dos Santos F. Wagner, Rosa C. Jose and Arantesa C. Eliane, A New Phospholipase A2 from Lachesis muta rhombeata: Purification, Biochemical and Comparative Characterization with Crotoxin B, Protein & Peptide Letters 2015; 22 (9) . https://dx.doi.org/10.2174/0929866522666150706112431
DOI https://dx.doi.org/10.2174/0929866522666150706112431 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |

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