Purification and characterization of active recombinant human napsin A.

@article{SchauerVukasinovic2000PurificationAC,
  title={Purification and characterization of active recombinant human napsin A.},
  author={Vesna Schauer-Vukasinovic and Daniel Bur and Eric A. Kitas and Daniel Schlatter and G{\'e}rard Ross{\'e} and Herr W. Lahm and Thomas Giller},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 9},
  pages={2573-80}
}
Recombinant human napsin A expressed in human embryonic kidney 293 cells was purified to homogeneity by a single-step procedure using part of napsin A propeptide as affinity ligand. N-Terminal amino-acid sequencing of the purified enzyme identified the mature form of napsin A. Treatment of purified napsin A with endoglycosidases F and H resulted in a decrease in its molecular mass from 39 kDa to approximately 37 kDa, confirming that napsin A is glycosylated. The kinetic properties were analyzed… CONTINUE READING