Biopolym. Cell. 1999; 15(4):292-296.
http://dx.doi.org/10.7124/bc.000528
Structure and Function of Biopolymers
Purification and properties of bee venom protease
1Protas A. F., 2Bondareva O. S., 2Muliavko N. O.
  1. Cross-industry company "Bereg"
    14, Karantinnaya Str., Odessa, Ukraine, 270014
  2. Prokopovich Institute of Apiculture UAAN
    19, Zabolotnogo Str., Kyiv, Ukraine, 03022

Abstract

See venom contains specific protease. It consists about 0.8–15 % 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), pHopt 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.
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References

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