Rapid on-membrane proteolytic cleavage for Edman sequencing and mass spectrometric identification of proteins

Electrophoresis. 2005 Nov;26(22):4243-51. doi: 10.1002/elps.200500206.

Abstract

A method for the rapid limited enzymatic cleavage of PVDF membrane-immobilized proteins is described. This method allows the fast characterization of PVDF blotted proteins by peptide mass fingerprinting (Henzel, W. J., Billeci, T. M., Stults, J. T., Wong, S. C., Grimley, C., Wantanabe, C., Proc. Natl. Acad. Sci. USA 1993, 90, 5011-5015), LC-MS/MS, or N-terminal sequencing and has been demonstrated on a range of proteins using a full complement of proteolytic enzymes. This technique allows the generation of proteolytic fragments between 5 and 60 min (depending on the enzyme employed), which is significantly faster than previously reported on-membrane digestion methods. To date, this on-membrane rapid digestion protocol has aided in the identification and confirmation of mutation sites in over 200 recombinant proteins.

MeSH terms

  • Amino Acid Sequence
  • Extracellular Matrix Proteins
  • Immunoglobulin Light Chains / chemistry
  • Mass Spectrometry / methods*
  • Membranes, Artificial*
  • Molecular Sequence Data
  • Neoplasm Proteins / chemistry
  • Peptide Hydrolases / metabolism*
  • Polyvinyls
  • Proteins / analysis*
  • Receptors, Interleukin / chemistry
  • Sequence Alignment
  • Sequence Analysis, Protein / methods*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Transforming Growth Factor beta / immunology

Substances

  • Extracellular Matrix Proteins
  • Immunoglobulin Light Chains
  • Membranes, Artificial
  • Neoplasm Proteins
  • Polyvinyls
  • Proteins
  • Receptors, Interleukin
  • SPON2 protein, human
  • Transforming Growth Factor beta
  • interleukin-20 receptor
  • polyvinylidene fluoride
  • Peptide Hydrolases