Purification, sequencing, and phylogenetic analyses of novel Lys-49 phospholipases A(2) from the venoms of rattlesnakes and other pit vipers.

@article{Tsai2001PurificationSA,
  title={Purification, sequencing, and phylogenetic analyses of novel Lys-49 phospholipases A(2) from the venoms of rattlesnakes and other pit vipers.},
  author={I. H. Tsai and Yi Hsuan Chen and Ying Wang and My Chau Tu and Anthony T. Tu},
  journal={Archives of biochemistry and biophysics},
  year={2001},
  volume={394 2},
  pages={236-44}
}
Basic phospholipase A(2) homologs with Lys49 substitution at the essential Ca(2+)-binding site are present in the venom of pit vipers under many genera. However, they have not been found in rattlesnake venoms before. We have now screened for this protein in the venom of rattlesnakes and other less studied pit vipers. By gel filtration chromatography and RP-HPLC, Lys49-phospholipase-like proteins were purified from the venoms of two rattlers, Crotalus atrox and Crotalus m. molossus, and five… CONTINUE READING

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