Abstract
Thiol-disulfide interchange enzyme which catalyzes the thiol-disulfide interchange was purified from cell-free extracts of Candida claussenii by acid treatment, ammonium sulfate fractionation, aqueous polymer two phase method (Dextran-PEG system), CM-Sephadex column chromatography, Sephadex G-100 and Sephadex G-200 gel filtrations. More than four active fractions were obtained on CM-Sephadex column. Further purification steps from one of these fractions resulted in two purified enzyme preparations D-1-1 and D-2 of which the increase in specific activities was 8150- and 8450-folds respectively, over the crude extract. Both purified enzymes were homogeneous in ultracentrifugal analysis.
