title: Comparative study of two arginine ester hydrolases, E-I and E-II from the venom of Crotalus ruber ruber (red rattlesnake).
abstract: 1. Two arginine ester hydrolases, E-I and E-II from the venom of Crotalus ruber ruber were isolated and characterized. 2. E-I and E-II have molecular weights of 32,000 and 33,000, and isoelectric points of 5.2 and 4.6, respectively. 3. E-I and E-II are active upon the glandular kallikrein substrate, but neither enzyme was shown to have plasma kallikrein substrate hydrolytic activity. 4. E-I has minimal fibrinogen-clotting activity. It was found to induce clotting by catalyzing the hydrolysis of only the A fibrinopeptide from the A alpha-chain of fibrinogen.
authors.affiliation: Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Mori
authors.forename: H
authors.initials: H
authors.lastname: Sugihara
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002942:Circular Dichroism; D003435:Crotalid Venoms / Q000032:analysis*; D005340:Fibrinogen / Q000378:metabolism; D007526:Isoelectric Point; D008970:Molecular Weight; D010455:Peptides; D013045:Species Specificity; D013379:Substrate Specificity; D014757:Viper Venoms / Q000032:analysis
chemical_list: D000596:Amino Acids; D003435:Crotalid Venoms; D010455:Peptides; D014757:Viper Venoms; D005340:Fibrinogen; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases