Crotalus scutulatus scutulatus crude venom was separated into two fractions by Concanavalin A Sepharose 4B affinity chromatography. The Concanavalin A-nonbinding fraction (F-l) exhibited phosphomonoesterase (orthophosphoric monoester phosphohydrolase EC 3.1 .3.2), phosphodiesterase, 5 '-nucleotidase (5 '-ribonucleotide phosphohydrolase EC 18.104.22.168), phospholipase A (phosphatidate 2-acylhydrolase EC 22.214.171.124), hyaluronidase (hyaluronate glycanohydrolase EC 3.2.1.d), N-benzoyl-Larginine ethyl esterase, p-toluenesulfonyl-L-arginine methyl esterase, L-amino acid oxidase (L-amino acid: O2 oxidoreductase [deaminating] EC 126.96.36.199), and caseinolytic activities. Thrombin-like and NAD nucleosidase (5 '-ribonudeotide phosphohydrolase EC 188.8.131.52) activities were not observed. DEAE Sephadex A-50 ion exchange chromatography by two stage elution of F-l yielded several fractions having proteinase activities. Proteinase activity was observed in the latter fractions of the first elution and in the fractions of the second elution.
Childs, C. K.; Hinson, Michael W.; Sifford, Dewey H.; and Johnson, Bob D.
"Concanavalin A-Nonbinding Enzymes of Crotalus scutulatus scutulatus Venom,"
Journal of the Arkansas Academy of Science: Vol. 40
, Article 7.
Available at: http://scholarworks.uark.edu/jaas/vol40/iss1/7