Fast characterization of intact proteins using a high-throughput eight-channel parallel liquid chromatography/mass spectrometry system

Rapid Commun Mass Spectrom. 2001;15(10):821-6. doi: 10.1002/rcm.276.

Abstract

The preparation of protein substrates requires that a large number of chromatographic fractions be analyzed for the presence of reactants, products and by-products. Analyses using linear matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) or single column liquid chromatography/mass spectrometry (LC/MS) have been inadequate because of mass resolution or throughput. Therefore, a high-throughput method employing an eight-channel parallel reverse-phase LC/MS system was developed. This system is capable of screening fractions from preparative ion-exchange chromatography with the required mass accuracy and throughput so that the protein purification process can be monitored in a relatively short period of time. As an example, the purification and analysis of an acylated protein with a molecular weight of 8.9 kDa is described and the detection of a contaminating by-product that differs in size by less than 20 Da is demonstrated. Using the current instrumentation and approach, it is practical to analyze 50 protein-containing fractions from column chromatography in less than 1 hour using parallel LC/MS.

MeSH terms

  • Acyl Carrier Protein / analysis
  • Acyl Carrier Protein / genetics
  • Acyl Carrier Protein / isolation & purification
  • Chromatography, High Pressure Liquid / instrumentation
  • Chromatography, High Pressure Liquid / methods*
  • Chromatography, Ion Exchange
  • Equipment Design
  • Molecular Weight
  • Protein Processing, Post-Translational
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / isolation & purification
  • Spectrometry, Mass, Electrospray Ionization / instrumentation
  • Spectrometry, Mass, Electrospray Ionization / methods*
  • Spectrophotometry, Ultraviolet
  • Time Factors

Substances

  • Acyl Carrier Protein
  • Recombinant Proteins