Biopolymers and cell. 1999; 15 (4): 292 - 296

Purification and properties of bee venom protease

A. F. Protas, O. S. Bondareva, N. O. Muliavko

See venom contains specific protease. It consists about 0.8—/.J % of total proteine-peptide fraction. The enzyme was purified with the help of benzamedine-sepharose and reverse-fase chromatography to the activity 110 U/mg. The protein is hydrophobic, its Mr is equal to 20 kDa (by gel-filtration), pHnft 4.5. Protease specifically binds to cell membrane in cooperative manner; the maximal binding ratio is 1.2. Enzyme has high substrate specifity for membrane proteins. It is concluded that protease is a specific toxic component of bee venom.