Abstract
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 3.1.3.5), phospholipase A (phosphatidate 2-acylhydrolase EC 3.1.1.4), 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 1.4.3.2), and caseinolytic activities. Thrombin-like and NAD nucleosidase (5 '-ribonudeotide phosphohydrolase EC 3.1.3.5) 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.
Recommended Citation
Childs, C. K.; Hinson, Michael W.; Sifford, Dewey H.; and Johnson, Bob D.
(1986)
"Concanavalin A-Nonbinding Enzymes of Crotalus scutulatus scutulatus Venom,"
Journal of the Arkansas Academy of Science: Vol. 40, Article 7.
Available at:
https://scholarworks.uark.edu/jaas/vol40/iss1/7
