황금 배양 세포로부터 Phospholipase A2의 분리

초록

It was previously reported that yeast elicitor transiently increased oleanolic acid and ursolic acid in Scutellaria baicalensis suspension cultures and also doubled phospholipase A2 (PLA2) activity. Thus, PLA2 was purified from the soluble fractions of S. baicalensis suspension cultures and the characters of the purified PLA2 were identified. The PLA2 was purified about 160 times compared with the starting soluble-protein extract from S. baicalensis suspension culture cells. The purified protein showed a molecular mass of about 43 kDa by SDS-PAGE. The purified plant PLA2 had a neutral pH optimum (pH 7.0) and required Ca 2+ for activity. The PLA2 activity was inhibited by mammalian PLA2 inhibitors such as 5,8,11,14-eicosatetraynoic acid (ETYA) and arachidonyl trifluoromethyl ketone (AACOCF3).

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