Phospholipases B from Japanese yellow hornet (Vespa xanthoptera) venom.
Two phospholipases B (Vx I and Vx II) were purified from the venom of the Japanese yellow hornet, Vespa xanthoptera, by sequential chromatography on Sephadex G-100, SP-Sephadex and Mono S columns. They are very similar to each other in molecular and enzymatic properties, though the specific activity of Vx I was one-fifth that of Vx II. They hydrolyze the acyl ester bonds at the 1-position of phosphatidylcholine and lysophosphatidylcholine, therefore, their enzymatic specificities were of the A1 and L1 types.
Takasaki
C
C
Department of Chemistry, Tohoku University, Sendai, Japan.
Fukumoto
M
M
D000596:Amino Acids / Q000032:analysis; D001514:Bee Venoms / Q000032:analysis*; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008245:Lysophospholipase / Q000032:analysis* / Q000302:isolation & purification; D008970:Molecular Weight; D017830:Octoxynol; D010740:Phospholipases / Q000032:analysis*; D010743:Phospholipids / Q000032:analysis; D011092:Polyethylene Glycols / Q000494:pharmacology; D013379:Substrate Specificity; D013997:Time Factors; D014862:Wasp Venoms / Q000032:analysis*
D000596:Amino Acids; D001514:Bee Venoms; D010743:Phospholipids; D014862:Wasp Venoms; D011092:Polyethylene Glycols; D017830:Octoxynol; D010740:Phospholipases; D008245:Lysophospholipase