A general, robust method for the quality control of intact proteins using LC–ESI-MS

A simple and robust method for the routine quality control of intact proteins based on liquid chromatography coupled to electrospray ionization mass spectrometry is presented

Gustav Sundqvist

2007

Scholarcy highlights

  • A simple and robust method for the routine quality control of intact proteins based on liquid chromatography coupled to electrospray ionization mass spectrometry is presented
  • A wide range of prokaryotic and eukaryotic proteins expressed recombinantly in Escherichia coli or Pichia pastoris has been analyzed with medium- to high-throughput with on-line desalting from multi-well sample plates
  • The method can be readily coupled with optimized chemical reduction and alkylation steps to facilitate the analysis of denatured or incorrectly folded proteins bearing cysteine residues, which otherwise form intractable multimers and non-specific adducts by disulfide bond formation

Need more features? Save interactive summary cards to your Scholarcy Library.