Isolation, amino acid sequence and biological characterization of an "aspartic-49" phospholipase A₂ from Bothrops (Rhinocerophis) ammodytoides venom.

@article{Clement2012IsolationAA,
  title={Isolation, amino acid sequence and biological characterization of an "aspartic-49" phospholipase A₂ from Bothrops (Rhinocerophis) ammodytoides venom.},
  author={Herlinda Clement and Vanessa Costa de Oliveira and Fernando Z. Zamudio and N{\'e}stor Rub{\'e}n Lago and Norma Adriana Valdez-Cruz and Melisa B{\'e}rnard Valle and Silvia Elvira Hajos and Alejandro Alag{\'o}n and Lourival Domingos Possani and Adolfo Rafael de Roodt},
  journal={Toxicon : official journal of the International Society on Toxinology},
  year={2012},
  volume={60 7},
  pages={1314-23}
}
A phospholipase enzyme was separated by chromatography from the venom of the snake Bothrops (Rhinocerophis) ammodytoides and characterized. The experimentally determined molecular weight was 13,853.65 Da, and the full primary structure was determined by Edman degradation and mass spectrometry analysis. The enzyme contains 122 amino acids residues closely stabilized by 7 disulfide bridges with an isoelectric point of 6.13. Sequence comparison with other known secretory PLA2 shows that the enzyme… CONTINUE READING