Elution patterns enzyme preparation from

Figure 1. Elution patterns of the ammonium sulfate-precipitated enzyme preparation from a DEAE-Sephadex A-50 column. (0) CMC-saccharifying activity (5-min incubation) of eluates diluted 60-fold, (O) Avicel-saccharifying activity (1-hr incubation), ( ) protein concentration measured in terms of the absorbance at 280 nm column 5.0 X 50 cm flow rate 20 mL/8 min one fraction 20 mL.

Fig. 1. Elution pattern of human plasma cholinesterase from DEAE-cellulose column solid line, absorbance at 280 nm broken line, enzyme activity. Partially purified enzyme preparation was placed on a DEAE-cellulose column (1.2 x 10 cm) and equilibrated with 0.02 mol/liter acetate buffer, pH 6.0. The column was washed with the same buffer containing 0.06 mmol/liter sodium chloride (up to 400 ml of effluent). Then (at single arrow) the enzyme was eluted with a linear gradient of sodium chloride and choline chloride ranging in concentration from 0.06 mmol/liter NaCl to 0.03 mmol/liter NaCl + 0.03 mol/liter choline chloride. At the double arrow, the buffer was changed to 0.02 mol/liter acetate buffer, pH 6.0, containing 0.2 mol/liter NaCl flow rate 25 ml per hour. (After Yoshida, Y2.)...

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