Cationic isotachophoresis separation of the biomarker cardiac troponin I from a high-abundance contaminant, serum albumin

Electrophoresis. 2014 Jul;35(14):2029-38. doi: 10.1002/elps.201400009. Epub 2014 Jun 5.

Abstract

Cationic ITP was used to separate and concentrate fluorescently tagged cardiac troponin I (cTnI) from two proteins with similar isoelectric properties in a PMMA straight-channel microfluidic chip. In an initial set of experiments, cTnI was effectively separated from R-Phycoerythrin using cationic ITP in a pH 8 buffer system. Then, a second set of experiments was conducted in which cTnI was separated from a serum contaminant, albumin. Each experiment took ∼10 min or less at low electric field strengths (34 V/cm) and demonstrated that cationic ITP could be used as an on-chip removal technique to isolate cTnI from albumin. In addition to the experimental work, a 1D numerical simulation of our cationic ITP experiments has been included to qualitatively validate experimental observations.

Keywords: Cardiac troponin I; Cationic isotachophoresis; Microfluidics; Preconcentration; Proteins.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Biomarkers / blood*
  • Cations
  • Computer Simulation
  • Humans
  • Isotachophoresis / methods*
  • Reproducibility of Results
  • Serum Albumin / chemistry
  • Serum Albumin / isolation & purification*
  • Troponin I / blood
  • Troponin I / chemistry
  • Troponin I / isolation & purification*

Substances

  • Biomarkers
  • Cations
  • Serum Albumin
  • Troponin I