Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry.

  title={Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry.},
  author={Martial Rey and P. Man and G. Brandolin and E. Forest and L. P{\'e}losi},
  journal={Rapid communications in mass spectrometry : RCM},
  volume={23 21},
  • Martial Rey, P. Man, +2 authors L. Pélosi
  • Published 2009
  • Chemistry, Medicine
  • Rapid communications in mass spectrometry : RCM
  • Hydrogen/deuterium (H/D) exchange coupled to mass spectrometry is nowadays routinely used to probe protein interactions or conformational changes. The method has many advantages, e.g. very low sample consumption, but offers limited spatial resolution. One way to higher resolution leads through the use of different proteases or their combinations. In the present work we describe recombinant production, purification and use of aspartic protease zymogen from Rhizopus chimensis, protease type XVIII… CONTINUE READING
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