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- W618630104 abstract "We previously reported that cultured mast cells expressed three discrete phospholipases A2 (PLA2s), one of which showed a remarkable preference for phospholipids bearing an arachidonoyl residue at the sn-2 position [M. Murakami, et al., J. Biochem., 111, 175 (1992)]. In the present study, we have purified and characterized this enzyme using rat mastocytoma RBL-2H3 as an enzyme source. The elution profiles of the arachidonoyl-preferential PLA2 activity of rat mastocytoma RBL-2H3 cells on several column chromatographies were indistinguishable from those of 85-kDa cytosolic PLA2 (cPLA2) characterized so far. The molecular mass of the partially purified PLA2 was estimated to be about 90 kDa by gel filtration and it hydrolyzed arachidonate-containing phospholipids preferentially in the presence of submicromolar Ca2+ concentrations. Furthermore, it was immunoprecipitated with an anti-rabbit cPLA2 antibody almost completely. From these observations, we have concluded that the arachidonoyl-preferential PLA2 in mast cells belongs to the cPLA2 family." @default.
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- W618630104 date "1994-01-01" @default.
- W618630104 modified "2023-09-24" @default.
- W618630104 title "Characterization of Cytosolic Phospholipase A2 in Rat Mastocytoma RBL-2H3." @default.
- W618630104 doi "https://doi.org/10.1248/bpb.17.47" @default.
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