Bothrops

Fibrinolytic effecting protease enzyme from the poison secretion (venom) of Bothrops atrox with glycoprotein structure. It has thrombin similarly endopeptidase activity. 

From an entirely different source, namely, the venom of the snake Bothrops iararaca, scientists at Squibb isolated a nonapeptide (SQ 20,881, LXXI) which is a potent inhibitor of the converting enzyme (99). 

In the first phase of their research, Squibb tested a short-chain peptide isolated from the venom of the viper Bothrops jararaca, with which Vane was working in the laboratory, in human volunteers and showed that it did, indeed, inhibit the conversion of angiotensin I to angiotensin II after intravenous injection. The peptide was also shown to reduce blood pressure in patients when injected. Since the vast majority of peptides cannot be absorbed from the GI tract, Squibb scientists set out to prepare a nonpeptide compound that could be used orally and manufactured at acceptable cost. The design of a true peptidomimetic that became orally active had not been accomplished at that time. Squibb then carried out... 

S American pit viper, Bothrops jararaca (Wied, 1824), Serpentes, Reptilia... 

It is a aqueous solution of haemocoagulase isolated from venom of Bothrops jararaca and B. atorox containing normal saline. It is indicated in primary and secondary postoperative internal and external haemorrhage. 

Since the acetone precipitation step is not applicable to all venoms, the decision of which method to use depends on the availability of the starting venom Crotalus adamanteus (35), Bothrops atrox (44), Heina-chatus haemachates (43), and Vipera lebetina (48). 

Enzyme Inhibitors from the Venom of Bothrops Jararaca Isolation, Elucidation of Structure, and Synthesis. Biochemistry. 1971,10, 4033 4039. 

VI. von Klobusitzky, D., and Konig, P., Biochemisehe Studien iiber die Gifte der Schlangengattung Bothrops, Arch, exptl. Pathol. Pharmakol. 192, 271 (1939). 

Ferreira s interest in the physiology of bradykinin led him in the early 1960s to search for substances that would inhibit its in vivo inactivation. The venom of the Brazilian arrowhead viper Bothrops jararaca generates bradykinin in plasma, and Ferreira discovered that the venom itself contained substances capable of potentiating bradykinin-induced contractions of isolated guinea pig ileum. He and Rocha e Silva called the active fraction of this venom the bradykinin-potentiating factor (BPF) (75). 

Ferreira, S.H., Bartelt, C., and Greene, F.J. 1970. Isolation of bradikinin potentiating peptides from Bothrops jararaca venom. Biochemistry 9, 2583-2593. 

Ondetti, M.A., Willimans, N.J., Sabo, E.F., Plusces, J., Weaver, E.R., and Kocy, O. 1971. Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure and synthesis. Biochemistry 19, 4033-4039. 

Jarariiagin, a snake venom fi om Bothrops jararaca, contains a metalloproteinase that cleaves the p, subunit (GPIIa) of the receptor complex, resulting in an inhibition of platelet adhesion to collagen" as well as an inhibition of early platelet signalling events in response to collagen, as demonstrated in the loss of pp72(syk) phosphorylation. 

Fan HW, Marcopito LF, Cardoso JL, Franca FO, Malaque CM, Ferrari RA, Theakston RD, Warrell DA. Sequential randomised and double blind trial of promethazine prophylaxis against early anaphylactic reactions to antivenom for bothrops snake bites. BMJ 1999 318(7196) 1451-2. 

Francis, B., Gutierrez, J. M., Lomonte, B., and Kaiser, I. I. (1991). Myotoxin 11 from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2. Arch. Biochem. Biophys. 284,352-359. 

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