Concanavalin A-Binding Enzymes of Crotalus scutulatus scutulatus Venom

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 3.1.3.2), phosphodiesterase, 5\u27-nucleotidase (5\u27-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-L-arginine ethyl esterase, p-toluenesulfonyl-L-arginine methyl esterase, L-amino acid oxidase (L-amino acid: 02 oxidoreductase [deaminating] EC 1.4.3.2), and caseinolytic activities. Thrombin-like and NAD nucleosidase (5\u27-ribonucleotide phosphohydrolase EC 3.1.3.5) 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

Concanavalin A-Nonbinding Enzymes of Crotalus scutulatus scutulatus Venom

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 \u27-nucleotidase (5 \u27-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 \u27-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

5\u27-Nucleotidase and Thrombin-Like Activities of Selected Crotalid Venoms

Thrombin-like activities were not observed inCrotalus basiliscus, C. molossus and C. scutulatus scutulatus crude venoms. 5\u27-Nucleotidase specific activities of 0.863, 0.273 and 5.520 units/mg of crude venom protein were observed inC. basiliscus, C. molossus and C. s. scutulatus venoms, respectively. Concanavalin ASepharose 4 B (Con A)affinitychromatography yielded two fractions from each of the crude venoms. Ineach instance, both fractions exhibited 5\u27-nucleotidase activities and the Con A-binding proteins had higher activities than the Con A-nonbinding proteins. 5\u27-Nucleotidase activities inthe DEAESephadex A-50 chromatographic fractions were localized in the first elution fraction and the last fraction(s) to elute. EDTAhad no effect on the 5\u27-nucleotidase activities ofthe crude venoms