Isolation and partial characterization of arginine ester hydrolase enzymes from the venom of Agkistrodon contortrix mokasen

CHED 213

Agatha Chester and Rodney L. Cate, rodney.cate@mwsu.edu. Department of Chemistry, Midwestern State University, 3410 Taft Blvd, Wichita Falls, TX 76308
Enzymes with arginine ester hydrolase activity have been partially characterized from the venom of Agkistrodon contortrix mokasen(ACM). Comparisons of the BAEE (N-benzoyl-L-arginine ethyl ester) hydrolytic activity of ACM venom and bovine trypsin indicated an enzymatic activities of 60:1 respectively. The BAEE active enzymes from the ACM venom were separated by a combination of gel permeation chromatogratography with BioGel P-100 and ion exchange chromatography with MacroPrep DEAE and CM resins. At least three separate arginine esterase enzymes have been identified and partially characterized by SDS gel electrophoresis.