Structural and functional characterization of a P-III metalloproteinase, leucurolysin-B, from Bothrops leucurus venom.

@article{Sanchez2007StructuralAF,
  title={Structural and functional characterization of a P-III metalloproteinase, leucurolysin-B, from Bothrops leucurus venom.},
  author={E. Sanchez and L. M. Gabriel and Sileia Gontijo and L. H. Gremski and S. S. Veiga and Karla S Evangelista and J. Eble and M. Richardson},
  journal={Archives of biochemistry and biophysics},
  year={2007},
  volume={468 2},
  pages={
          193-204
        }
}
Leucurolysin-B (leuc-B) is an hemorrhagic metalloproteinase found in the venom of Bothrops leucurus (white-tailed-jararaca) snake. By means of liquid chromatography consisting of gel filtration on Sephracryl S-200, S-300 and ion-exchange on DEAE Sepharose, leuc-B was purified to homogeneity. The proteinase has an apparent molecular mass of 55kDa as revealed by the reduced SDS-PAGE, and represents approximately 1.2% of the total protein in B. leucurus venom. The partial amino acid sequence of… Expand
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