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Supplementary Information
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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])
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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]).
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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]).
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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])
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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])
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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]).
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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])
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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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