Peptide maps of labeled poliovirus proteins after two‐dimensional analysis by limited proteolysis and electrophoresis in sodium dodecyl sulfate

This is the authors' abstract. We don't add key points for this paper.

A simple technique for characterization and identification of proteins after high resolution two‐dimensional (2D) electrophoresis is described. Poliovirus proteins were separated by 2D analysis and then subjected to llimited proteolysis in sodium dodecyl sulfate (SDS) by alfa‐Chymotrypsin or Staphylococcus V8 protease. The cleavage products were analyzed by SDS‐polyacrylamide gel electrophoresis (SDS‐PAGE). The pattern of peptides obtained was characteristic for a given protein and for the protease used and was highly reproducible. Alfa‐Chymotrypsin produced fewer and larger peptides and was suitable for large poliovirus proteins. Staphylococcus V8 protease yielded smaller peptides and therefore showed a higher degree of discrimination between the poliovirus proteins analyzed. A precursor product relationship for a number of poliovirus proteins was determined by this simple technique.

May aid lab-based viral protein mapping; leaves open clinical translation beyond animal models.