Decrease of dynamic range of proteins in human plasma by ampholine immobilized polymer microspheres

Anal Chim Acta. 2014 May 15:826:43-50. doi: 10.1016/j.aca.2014.04.004. Epub 2014 Apr 8.

Abstract

A novel protein sample pretreatment method based on ampholine immobilized polymer microsphere (ampholine@PM) was developed for the fractionation of intact proteins prior to protein digestion and peptide analysis to reduce the dynamic range of human plasma proteome. After incubation with our prepared ampholine@PM, the captured plasma proteins were successively desorbed by 2M NaCl, 100mM glycine-hydrochloric acid, and 30% (v/v) acetonitrile with 0.1% (v/v) trifluoroacetic acid. The SDS-PAGE results showed the protein dynamic range in such three fractions was obviously reduced as compared with the native plasma. On-particle digestion was ultimately performed to release all proteins retained on ampholine@PM. Followed by MuPIT analysis, the number of identified proteins in plasma was improved by 75% after ampholine@PM treatment. Furthermore, the spectral count of 9 high abundance proteins was decreased by 37.6-97.2%, and the identified low abundance protein (<100ngmL(-1)) number was increased from 4 to 17. These results demonstrated that the fractionation by ampholine@PM could efficiently decrease the protein dynamic range in abundance, beneficial to achieve the deep coverage identification of human plasma proteome.

Keywords: Ampholine; Fractionation; Human plasma; Protein dynamic range.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blood Proteins / chemistry*
  • Chemical Fractionation*
  • Humans
  • Microspheres*
  • Polyamines / chemistry
  • Polymers / chemistry*

Substances

  • Blood Proteins
  • Polyamines
  • Polymers
  • Ampholine