Cationic isotachophoresis separation of the biomarker cardiac troponin I from a high-abundance contaminant, serum albumin.
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.
Gene and Linda Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, USA.
Thomas
T
Jacroux
Danny
D
Bottenus
Bennett
B
Rieck
Cornelius F
CF
Ivory
Wen-Ji
WJ
Dong
D015415:Biomarkers / Q000097:blood*; D002412:Cations; D003198:Computer Simulation; D006801:Humans; D057625:Isotachophoresis / Q000379:methods*; D015203:Reproducibility of Results; D012709:Serum Albumin / Q000737:chemistry / Q000302:isolation & purification*; D019210:Troponin I / Q000097:blood / Q000737:chemistry / Q000302:isolation & purification*
D015415:Biomarkers; D002412:Cations; D012709:Serum Albumin; D019210:Troponin I
Cardiac troponin I; Cationic isotachophoresis; Microfluidics; Preconcentration; Proteins