Supplementary Information

Figure S1: Separation of a mixture of proteins (A) in an untreated and (B and C) in treated capillaries with fluorescence detection. Injection: (1) lysozyme, (2) trypsin and (3) chymotrypsinogen. (A) Untreated fused-silica capillary; buffer, 0.01 M KH2P04, pH = 6.8 (B) PEG-coated capillary; buffer, 0.01 M KH2P04, pH = 6.8. (C) PEG-coated capillary; buffer, 0.05 M KH2P04, pH = 4.1. (With permission from ref. [27])

Figure S2: Electropherogram of a mixture of seven proteins. Injection, 10 s, 10 kV. KH2P04 concentration, 0.03 M, pH = 3.8. 1 = cytochrome c; 2 = lysozyme; 3 = myoglobin; 4 = trypsin; 5 = ribonuclease; 6 = trypsinogen: 7 = chymotrypsinogen. (With permission from ref. [27]).

Figure S3: Micellar electrokinetic chromatograms of the sample mixture obtained with capillaries with different surface modifications: (a) untreated fused-silica capillary from Supelco, (b) C18 coated capillary from Supelco, (c) methyl silicone coated capillary from Chrompack and (d) polyethylene glycol coated capillary from Chrompack. Background electrolyte, 10 mM TRIS-phosphoric acid at pH 7.0 with 50 mM SDS. Applied voltage, 20 kV. (1) resorcinol, (2) phenol, (3) p-nitroaniline, (4) p-cresol, (5) 2,6-xylenol, (6) toluene, (7) 1,2-xylol, (8) propylbenzene and (9) Sudan III (with permission from ref. [35]).

Figure S4: Electropherogram of a mixture of 10 metal ions (1x10-4 mol dm-3) in 0.01 mol dm-3 creatinine plus 1% m/v PEG300000 (pH 4.27). 1, Potassium; 2, barium; 3, magnesium; 4, zinc; 5, lithium; 6, lead. Experimental conditions: 0.01 mol dm-3 creatinine at pH 4.27; neutral marker, water; field strength, 500 V cm-1 ; direction of electroosrnotic flow, is towards the cathode. (With permission from ref. [33])

Figure S5: Isotachopherograms for the separations of alkali and alkaline earth metal cations. Only the records from the analytical column are given. (A) Leading electrolyte without PEG; (B) leading electrolyte containing water-PEG (55:45). The driving currents were 250 and 45 PA in the preparation and analytical columns, respectively. R, t = increasing resistance and time, respectively. u = Unidentified impurity originating from the terminating electrolyte. (With permission from ref. [34])

Figure S6: Profile of hemoglobin with PEG600 escorting chromatography. Chromatographic column was packed with 10mL Q Sepharose Big Beads; equilibrium buffer: 10 mmol L-1 PBS, pH 7.8; loading quantity: 100 mL protein with a concentration of 200mgmL-1; loading rate: 25 cm h-1, 5 min later the flow rate was raised to 75 cm h-1, rinsed until hemoglobin flow through completely (45 min later), absorbed hemoglobin and impurities were eluted by 10 mmol L-1 PBS containing 1 mol L-1 NaCl at a flow rate of 150 cm h-1. B) Bioactivity of hemoglobin after PEG escorting chromatography. (With permission from ref. [45]).

Figure S7: Change in retention of cations with PEG 20000 concentration in methanolic mobile phase. Mobile phase contains 0.1 M NH4CI. Stationary phase, GS-320H. (With permission from ref. [50])

Figure S8: Chromatograms of a blank beer (left) and a naturally contaminated sample of beer containing 0.10 ng/ml ochratoxin A (OTA) (right) following the extraction and clean-up procedures proposed in [56]. (With permission from ref. [56])

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