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Purification of acid proteinases from calf brain.

The purification was begun with acetone precipitation of minced brain tissue with subsequent proteinase extraction with 0.2 M sodium formate buffer (pH 3.5), reprecipitation with acetone and dialysis. Chromatographic separation on Sephadex G-200, DEAE-Sephadex A-50 and CM-cellulose was carried out in that order. Upon ion-exchange chromatography multiple forms of acid proteinases emerged; two of them were obviously identical with cathepsin D (EC 3.4.23.5), and two of them exhibited properties of cathepsin B (EC 3.4.22.1).