황금 배양 세포로부터 Phospholipase A2의 분리 = Purification of Phospholipase A2 from Scutellaria baicalensis Suspension Cells

다국어 초록 (Multilingual Abstract)

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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