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KMID : 0616120090400010013
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Korean Journal of Pharmacognosy
2009 Volume.40 No. 1 p.13 ~ p.17
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Purification of Phospholipase A2 from Scutellaria baicalensis Suspension Cells
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Ma Choong-Je
Kim Dae-Kyung
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Abstract
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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 Ca2+ 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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KEYWORD
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arachidonyl trifluoromethyl ketone, 5, 8, 11, 14-eicosatetraynoic acid, phospholipase A2, Scutellaria baicalensis
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