Properties of the arginine esterases from Bitis nasicornis (horned adder) venom.

@article{Joubert1984PropertiesOT,
  title={Properties of the arginine esterases from Bitis nasicornis (horned adder) venom.},
  author={Francois J. Joubert and Edwin Howard Merrifield},
  journal={Hoppe-Seyler's Zeitschrift fur physiologische Chemie},
  year={1984},
  volume={365 10},
  pages={
          1219-25
        }
}
Five forms of arginine esterase (DE-2 to DE-6) were purified from Bitis nasicornis venom by gel filtration on Sephadex G-50, followed by ion exchange chromatography on CM-cellulose and DEAE-sepharose. They contain 17.6 to 23.1% of carbohydrate, 242 to 244 amino acids including 14 half-cystine residues and have molecular masses of about 38 kDa. The enzymes have a high esterolytic activity towards N alpha-benzoyl-L-arginine ethyl ester but show no proteolytic activity against Azocoll and no… 
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