The purification of acid phosphatase from honey bee venom (Apis mellifica).
Acid phosphatase from bee venom was purified by a combination of saturated ammonium sulphate precipitation, gel filtration and ion exchange chromatography. The final product which is a glycoprotein contained less than 0.1% phospholipase A2 or hyaluronidase activity and existed in two molecular weight (96,000 and 45,000) forms. Acid phosphatase is a potent allergen, in bee venom allergic patients, which is capable of releasing histamine from sensitized human basophils and of inducing a wheal and flare reactions in sensitized human skin.
Barboni
E
E
Department of Chemistry, University College London, U.K.
Kemeny
D M
DM
Campos
S
S
Vernon
C A
CA
D000135:Acid Phosphatase / Q000302:isolation & purification*; D000645:Ammonium Sulfate; D000818:Animals; D001514:Bee Venoms / Q000032:analysis*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006863:Hydrogen-Ion Concentration
D001514:Bee Venoms; D000135:Acid Phosphatase; D000645:Ammonium Sulfate