Structural characterization and neuromuscular activity of a new Lys49 phospholipase A2 homologous (Bp-12) isolated from Bothrops pauloensis snake venom

Priscila Randazzo-Moura, L. A. Ponce-Soto, Léa Rodrigues-Simioni, Sérgio Marangoni

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

11 Citas (Scopus)

Resumen

Bp-12 was isolated from Bothrops pauloensis snake venom in only one chromatographic step in reverse phase HPLC on μ-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 PLA2. The sequence of Bp-12 contains 122 amino acid residues: SLFELGKMIL QETGKNPAKS LGAFYCYCGW GSQGQPKDAV DRCCYVHKCC YKKITGCNPK KDRYSYSWKD KTLVCGEDNS CLKELCECDK AVAICLRENL NTYNKKYRYF LKPLCKKADA AC, with a pI value of 8.55 and with a high homology with Lys49 PLA2 from other snake venoms. In mouse phrenic nerve-diaphragm, the time needed for 50% paralysis was: 45 ± 6 min (1.4 μM) and 16 ± 6 min (3.6 μM). 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.

Idioma originalInglés
Páginas (desde-hasta)355-362
Número de páginas8
PublicaciónProtein Journal
Volumen27
N.º6
DOI
EstadoPublicada - set. 2008
Publicado de forma externa

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