Abstract
THE well-known blood-clotting activity of the venom from snakes of various species of the genus Bothrops has been attributed to its proteolytic activity1, although Michl2 (using paper electrophoresis) and Holz and Raudonat3 (using fractional precipitation with ammonium sulphate) have presented evidence against this point of view. The latter authors obtained a fraction, which they called “Koagulin”, with a strong blood-clotting activity but only slight proteolytic activity when hæmoglobin was used as substrate. More recently, it has been shown that there exist at least two proteolytic enzymes in the venom of Bothrops jararaca: one of them is thermolabile4 and is precipitated at 50 per cent saturation with ammonium sulphate5, while the other is stable to heat4 and is precipitated at 70 per cent saturation with ammonium sulphate5. The latter enzyme has been isolated in a fairly pure state and has been called Bothrops protease A (ref. 6).
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References
Janzky, B., Arch. Biochem., 28, 139 (1950).
Michl, H., Monatsh. f. Chem., 85, 1240 (1954).
Holz, P., and Raudonat, H. W., Arch. Exp. Pathol. Pharmakol., 229, 113 (1956).
Hamberg, U., and Rocha e Silva, M., Ciência e Cultura, 8, 176 (1956).
Henriques, O. B., Lavras, A. A. C., and Fichman, M., Ciência e Cultura, 8, 240 (1956).
Henriques, O. B., Lavras, A. A. C., Fichman, M., Mandelbaum, F. R., and Henriques, S. B., Biochem. J., 68, 597 (1958).
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HENRIQUES, O., MANDELBAUM, F. & HENRIQUES, S. Blood-clotting Activity of the Venom of Bothrops jararaca. Nature 183, 114–115 (1959). https://doi.org/10.1038/183114a0
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DOI: https://doi.org/10.1038/183114a0
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