Purification, characterization and substrate specificity of rat pancreatic elastase II.

@article{Szilagyi1995PurificationCA,
  title={Purification, characterization and substrate specificity of rat pancreatic elastase II.},
  author={Corinne Szilagyi and P D Sarfati and Lucien Pradayrol and Jean A. Morisset},
  journal={Biochimica et biophysica acta},
  year={1995},
  volume={1251 1},
  pages={55-65}
}
A somatostatin-14-degrading activity has been purified to homogeneity from rat pure pancreatic juice. This proteinase was concentrated more than 350-fold in a four-step procedure including ion-exchange and gel filtration. The final preparation contained a single protein with a molecular weight (M(r)) of approx. 29,000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The determination of its NH2-terminal sequence led us to conclude that the purified proteinase… CONTINUE READING