TY  - JOUR
A1  - Carregari, Victor Corasolla
A1  - Floriano, Rafael Stuani
A1  - Rodrigues-Simioni, Lea
A1  - Winck, Flavia V.
A1  - Baldasso, Paulo Aparecido
A1  - Ponce-Soto, Luis Alberto
A1  - Marangoni, Sergio
T1  - Biochemical, Pharmacological, and Structural Characterization of New Basic PLA(2) Bbil-TX from Bothriopsis bilineata Snake Venom
JF  - BioMed research international
N2  - Bbil-TX, a PLA(2), was purified from Bothriopsis bilineata snake venom after only one chromatographic step using RP-HPLC on mu-Bondapak C-18 column. A molecular mass of 14243.8 Da was confirmed by -Tof ltima API ESI/ MS (TOF MS mode) mass spectrometry. The partial protein sequence obtained was then submitted to BLASTp, with the search restricted to PLA(2) from snakes and shows high identity values when compared to other PLA(2)s. PLA(2) activity was presented in the presence of a synthetic substrate and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0 and 25-37 degrees C. Maximum PLA(2) activity required Ca2+ and in the presence of Cd2+, Zn2+, Mn2+, and Mg2+ it was reduced in the presence or absence of Ca2+. Crotapotin from Crotalus durissus cascavella rattlesnake venom and antihemorrhagic factor DA2-II from Didelphis albiventris opossum sera under optimal conditions significantly inhibit the enzymatic activity. Bbil-TX induces myonecrosis in mice. The fraction does not show a significant cytotoxic activity in myotubes and myoblasts (C2C12). The infiammatory events induced in the serum of mice by Bbil-TX isolated from Bothriopsis bilineata snake venom were investigated. An increase in vascular permeability and in the levels of TNF-a, IL-6, and IL-1 was was induced. Since Bbil-TX exerts a stronger proinfiammatory effect, the phospholipid hydrolysis may be relevant for these phenomena.
Y1  - 2013
U6  - https://doi.org/10.1155/2013/612649
SN  - 2314-6133
SN  - 2314-6141
PB  - Hindawi Publishing Corp.
CY  - New York
ER  -