Purification and partial characterization of a thrombin-like/gyroxin enzyme from bushmaster (Lachesis muta rhombeata) venom.

@article{Aguiar1996PurificationAP,
  title={Purification and partial characterization of a thrombin-like/gyroxin enzyme from bushmaster (Lachesis muta rhombeata) venom.},
  author={Aniesse Silva Aguiar and Carlos Roberto Alves and A R Melgarejo and Salvatore Giovanni-De-Simone},
  journal={Toxicon : official journal of the International Society on Toxinology},
  year={1996},
  volume={34 5},
  pages={555-65}
}
The acidic coagulating enzyme of the L. m. rhombeata venom was purified to homogeneity using one step on preparative isoelectric focusing followed by gel permeation on a high performance liquid chromatography system. The enzyme focused with pIs 3.1-5.0 and had a molecular mass of 47,000 mol. wt as determined by high performance liquid gel-filtration chromatography and about 45,000 mol. wt as judged by sodium dodecyl sulfate-polyacrylamide-gel electrophoresis. The enzyme is a glycoprotein… CONTINUE READING

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