Starch phosphorylase was partially purified from cabbage leaves using ammonium sulfate fractionation and DEAB-cellulose chromatography. The enzyme showed optimum activity at pH 6.0 and 40°C. It showed absolute specificity for glucose-1-phosphate and utilized starch or amylose as primer with equal efficiency. This was followed by amylopectin and glycogen. However, Schardinger dextrin and cellulose failed to act as primer. L-tyrosine, non-competitively, inhibited the enzyme activity.
