Crotalus scutulatus scutulatus crude venom was separated into two fractions by Concanavalin A Sepharose 4B affinity chromatography. The proteins binding to Con A exhibited phosphomonoesterase (orthophosphoric monoester phosphohydrolase EC 126.96.36.199), phosphodiesterase, 5'-nucleotidase (5'-ribonucleotide phosphohydrolase EC 188.8.131.52), phospholipase A(phosphatidate 2-acylhydrolase EC 3.1.1 .4), hyaluronidase (hyaluronate glycanohydrolase EC 3.2.1 d), N-benzoyl-L-arginine ethyl esterase, p-toluenesulfonyl-L-arginine methyl esterase, L-amino acid oxidase (L-amino acid: 02 oxidoreductase [deaminating] EC 184.108.40.206), and caseinolytic activities. Thrombin-like and NAD nucleosidase (5'-ribonucleotide phosphohydrolase EC 220.127.116.11) activities were not observed. The crude venom and the fraction containing the glycoproteins which bound to Con A were fractionated by DEAE Sephadex A-50 ion exchange chromatography. Each of these samples yielded fractions having caseinolytic activities.
Hinson, Michael W.; Childs, C. K.; Johnson, Bob D.; and Sifford, Dewey H.
"Concanavalin A-Binding Enzymes of Crotalus scutulatus scutulatus Venom,"
Journal of the Arkansas Academy of Science: Vol. 39
, Article 13.
Available at: http://scholarworks.uark.edu/jaas/vol39/iss1/13