Iontosorb DEAE

is a weakly basic anion exchange based on Bead Cellulose with 2-diethylamino-ethyl functional group:

The total volume exchange capacity of this sorbent strongly depends on its porosity and moves in the range 0.13 to 0.63 mmol/ml. To this interval the mass capacity in the range 2.2 to 2.8 mmol/g dry matter is adequate. The water content in the sorbent is given by its porosity, which can be varied by conditions during synthesis. according to the customer´s demands. The water content can vary in the range 3.7 to 11.4 g H₂O/g, (78 - 92 % H₂O). The B.V. (Bead Volume) moves in the range 7.1 to 20.3 ml/g according to the chosen porosity of the anion exchanger.

Iontosorb DEAE can be used in analytical chemistry and preparative chromatographic separations of proteins, nucleic acids and their components, peptides, amino acids, hormones, enzymes, RNA, polar lipids, haemoglobin and others natural substances as well as a scavenger in the preparation of ultra-pure water [ref. 13] and sorption of humic acids from water [ref. 14].

Applications of Iontosorb DEAE

Scientific Papers of the Prague Institute of Chemical Technology H 18 (1983) 137-145

Sorption of Gold on Iontosorb DEAE and Iontosorb DEAHP in dependence on the Concentration of HCl in the Sorption Solution

(Qa - practical specific capacity of the Iontosorb, mmol Au per g dry Iontosorb)

Curves: 1 - Iontosorb DEAE, 2 - Iontosorb DEAHP

Sorption and Desorption Breakthroung Curves of Copper on the Iontosorb DEAE and Iontosorb DEAHP

Amount of exchanger correspound to 5.1 or 6.0 of dry substance for DEAE or DEAHP, respectively;

column: d = 10 mm, Ve = 30 ml; solution: HCl (c = 0.05 mol/l);

V/Vc - ration of the efluent volume (V) to the column packing volume (Vc),

c/c₀ - ratio of the copper concentration in the efluent (c) and in the influent (c₀ = 50 mmol/l)

Curves: 1 - Iontosorb DEAE, 2 - Iontosorb DEAHP

Sorption Breakthrough Curves of Gold on the Iontosorb DEAE and Iontosorb DEAHP

Amount of exchanger corresponds to 0.511 or 0.528 g of dry substance for DEAE and DEAHP, respectively

column: d = 4 mm, Vc = 3 ml; solution HCl (c= 0.1 mol/l)

V/Vc - ration of the efluent volume (V) to the column packing volume (Vc),

c/c₀ - ratio of the gold concentration in the efluent (c) and in the influent (c₀ = 5 mmol/l)

Curves: 1 - Iontosorb DEAE, 2 - Iontosorb DEAHP

Original articles as full texts are available in the information CD of the firm Iontosorb.

ISOLATION AND CHARACTERISATION OF THE PROTEOLITIC ENZYMES OF CARP HEPATOPANCREAS

Chromatography of the extract of carp hepatopancreas free of Leu-aminopeptidase on Iontosorb DEAE at pH 7.9

(numbers 1-9 show pooled fractions)

Trypsin and chmotrypsin activity in pooled fractions obtained from Iontosorb DEAE column (pH 7.9)

The Column 2 x 10 mm equilibrated with 10 mM Tris-HCl pH 7.9 buffer containing 10 mM calcium chloride, flow rate was 60 ml/h

Bound enzymes were eluted stepwise with 0.14, 0.3 and 1 M HCl in the above buffer.

Original articles as full texts are available in the information CD of the firm Iontosorb.

USE OF BEAD CELLULOSE DERIVATIVES TO ISOLATION OF BACTERIAL ALKALINE PROTEINASE BY COLUMN LIQUID CHROMATOGRAPHY

P. Gemeiner, V. Spanik, A. Snajdrova, E. Stratilova, M. Horvathova, D. Hagarova and O. Markovic

Semi preparative ion exchange chromatography of alkaline proteinase on Iontosorb DEAE

The column 21 x 132 mm was equilibrated and eluted using Tris-HCl buffer, 116 mg lyophilizate dissolved in 10 mL Tris-HCl buffer was loaded and eluted at 0.5 mL/min;

N - fraction number; A₂₈₀ -proteins (circles), A₂₅₃ - nucleo-compounds (triangles), A₆₂₀/h - proteolytic activity (squares)

Semi preparative ion exchange chromatography of alkaline proteinase on Iontosorb DEAE

The column 41.5 x 400 mm was equilibrated and eluted using Tris-HCl buffer, the sample was 1.16 g alkaline proteinase in 10 mL equilibration buffer, 20 mL fractions were collected;

N - fraction number, A₂₈₀ - proteins, A₂₅₃ - nucleo-components (triangles), A₆₂₀/h - proteolytic activity (squares)

Maximum proteolytic activity was in the combined fractions 22 - 24.

Elution profiles of crude (top) and purified (bottom) alkaline proteinase after size-exlusion chromatography on Superose 12 HR 10/30 column using FPLC set-up

The column was loaded with 0.26 (top) and 0.36 (bottom) mg protein, respectively, in 0.2 mL Tris-HCl (20 mmol/L, pH 8.8). The crude sample (top) was the lyophilizate after fermentation, the "buttom" sample was the mixture of fractions 22 - 24 after preparative Iontosorb DEAE (the above given figure);

elution was with 50 mmol/L phosphate buffer (pH 7) containing 150 mmol/L NaCl, flow rate was 0.5 mL/min; V - volume (mL)

Original articles as full texts are available in the information CD of the firm Iontosorb.

COMPETITIVE ELUTION OF LACTATE DEHYDROGENASE FROM CIBACRON BLUE CELLULOSE (Iontosorb BLUE-2) WITH CIBACRON BLUE-DEXTRAN

Elution profile of LDH on Iontosorb DEAE column

Column 15 x 115 mm equilibrated with 20 mM phosphate buffer (pH 8.5); linear gradient elution with 0-0.1 M (NH₄)₂SO₄ in phosphate bufer; 10 ml fractions were collected and analysef for (empty circle) LDH activity and (full circle) protein. The two main fractions (1, 10 ml; 2, 90 ml) were pooled.

Original articles as full texts are available in the information CD of the firm Iontosorb.

Technical Parameters

Porozity Type	Particle Size [ um ]
DEAE 100	30 - 50
	50 - 80
	80 - 100
	100 - 250
	250 - 500
DEAE 200	50 - 80
	80 - 100
	100 - 250
	250 - 500
DEAE 500	50 - 80
	80 - 100
	100 - 250
	250 - 500