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|Type:||Artigo de periódico|
|Title:||Structural Characterization and Neuromuscular Activity of a New Lys49 Phospholipase A(2) Homologous (Bp-12) Isolated from Bothrops pauloensis Snake Venom|
|Abstract:||Bp-12 was isolated from Bothrops pauloensis snake venom in only one chromatographic step in reverse phase HPLC on mu-Bondapack C-18. The molecular mass of 13,789.56 Da was determined by mass spectrometry. The amino acids composition showed that Bp-12 presented high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical of a basic PLA(2). The sequence of Bp-12 contains 122 amino acid residues: SLFELGKMIL QETGKNPAKS LGAFYCYCGW GSQGQPKDAV DRCCYVHKCC YKKITGCNPK KDRYSYSWKD KTLVCGEDNS CLKEL CECDKAVAICLRENL NTYNKKYRYFLKPLCKKADA AC, with a pI value of 8.55 and with a high homology with Lys49 PLA(2) from other snake venoms. In mouse phrenic nerve-diaphragm, the time needed for 50% paralysis was: 45 +/- 6 min (1.4 mu M) and 16 +/- 6 min (3.6 mu M). Bp-12 can induce indirect and directly blocked evoked twitches, even in the preparations in which Ca2+ is replaced by Sr2+, being the addition of d-tubocurarine required for direct blocking. These results identify Bp-12 as a new member of the Lys49 PLA(2) family and shows that this toxin might contribute to the effects of the crude venom on the neuromuscular junction.|
|Citation:||Protein Journal. Springer, v. 27, n. 6, n. 355, n. 362, 2008.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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