LC-MS/MS Analysis of the Active Fraction DEAE-2 Purified from the Artemisia annua Crude Enzyme

The crude enzyme extract from Artemisia annua was subjected to catalytic activity-guided purification and fractionation, yielding the active fraction DEAE-2, which demonstrated the biological function of catalyzing the interconversion between artemisinic acid and dihydroartemisinic acid. Proteomic identification of DEAE-2 was performed to uncover the functional enzymes responsible for this activity.