Effect of bilineobin, a thrombin-like proteinase from the venom of common cantil (Agkistrodon bilineatus)

A Novel Venombin B fromAgkistrodon contortrix contortrix: Evidence for Recognition Properties in the Surface around the Primary Specificity Pocket Different from Thrombin

“…In contrast, contortrixobin releases FPB preferentially from human fibrinogen, at least under the experimental conditions used in this work (4 times quicker than FPA). Most venombins release FPA from fibrinogen, whereas only a few preferentially attack its -chains, among these, venombins B purified from Agkistrodon contortrix contortrix (73), Agkistrodon halys pallas (74), Trimeresurus okinaVensis (75); Crotalus atrox (76), Vipera lebetina (77), Agkistrodon bilineatus (78), and Agkistrodon halys blomhoffii (50), in addition to contortrixobin reported in this work. The cleavage of the fibrinogen -chains produced by these venombins does not occur always at the site typically recognized by thrombin and contortrixobin (i.e., ArgB 14), but in some cases at another site (i.e., ArgB 42) as described for halystase (50) and protease III from Crotalus atrox (79).…”

Venomics of Vipera berus berus to explain differences in pathology elicited by Vipera ammodytes ammodytes envenomation: Therapeutic implications

“…Vbb SVSPs, with apparent molecular masses of 25, 35, 40 and 55 kDa, were identified in PRLP-S fractions 8 to 14 by similarity to SVPSs from related snakes, Vaa, Macrovipera lebetina (M. lebetina), Crotalus atrox (C. atrox), Agkistrodon contortrix contortrix (A. c. contortrix) and Trimeresurus stejnegeri (T. stejnegeri). These Vbb SVSPs may thus exert thrombin-like, fibrinogenolytic and kallikrein-like activities [34][35][36][37][38]. However, as demonstrated in Fig.…”

Expression, Refolding, and Activity of a Recombinant Nonhemorrhagic Snake Venom Metalloprotease

“…One group of enzymes is usually involved in activation of the coagulation cascade, leading to clot formation. This group includes the thrombin-like enzymes (1,2), the prothrombin activator factors, and the factor X activators (3)(4)(5). Conversely, snake venom metalloproteases (svMP, EC 3.4.24.42) 2 are fibrin-(ogen)olytic enzymes, and the incubation of plasma with these enzymes usually makes it incoagulable (6).…”

“…This group includes the thrombin-like enzymes (1,2), the prothrombin activator factors, and the factor X activators (3)(4)(5). Conversely, snake venom metalloproteases (svMP, EC 3.4.24.42) 2 are fibrin-(ogen)olytic enzymes, and the incubation of plasma with these enzymes usually makes it incoagulable (6). Several metalloproteases have been purified from snake venoms and characterized at both the primary and the tertiary structural levels (7)(8)(9)(10).…”