Abstract
Creatinine deiminase (EC 3. 5. 4. 21) was formed in large quantities in the cells of Corynebacterium lilium ATCC 15990, aerobically grown on creatinine as a sole source of nitrogen. The creatinine deiminase was purified and crystallized from the cell extracts by a procedure involving fractionation with ammonium sulfate, treatment with protamine, and chromatographies on DEAE-cellulose, Sephadex G-100, and hydroxylapatite. This process resulted in a 2400-fold increase in specific activity with a recovery of 9.1%. The crystalline enzyme was homogeneous on acrylamide gel electrophoresis and ultracentrifugation (s20, W=10.44S).
