Purification and properties of bee venom protease

Authors

  • A. F. Protas Cross-industry company "Bereg" 14, Karantinnaya Str., Odessa, Ukraine, 270014 Author
  • O. S. Bondareva Prokopovich Institute of Apiculture UAAN 19, Zabolotnogo Str., Kyiv, Ukraine, 03022 Author
  • N. O. Muliavko Prokopovich Institute of Apiculture UAAN 19, Zabolotnogo Str., Kyiv, Ukraine, 03022 Author

DOI:

https://doi.org/10.7124/bc.000528

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.

References

Ahunov A. Proteolytic enzymes snake venoms the Central Asian Issues. gerpentologii. Leningrad: Nauka, 1973. p 34—36.

Pokrovsky A. Enzyme mechanism certain intoxications (attempt enzyme classification of poisons). Uspekhi biologicheskoy khimii. 1962;4:61—80.

Orlov BN. Zootoksikologiya. M.: Vysshaya shkola 1985. 228 p.

Ivanov Ts, Shkenderov S. Bees products. Sofia Zemizdat, 1985. 226p.

Protas AF, Chaialo PP. Isolation of a histone-specific proteinase from brain cell nuclei of rats. Ukr Biokhim Zh. 1991;63(5):99-102.

Benzamidine Sefarose 6B. Pharmacia. Data Sheet.

biopolym.cell-1999-15-4-cover.png

Downloads

Published

1999-07-20

Issue

Vol. 15 No. 4 (1999)

Section

Structure and Function of Biopolymers