Abstract
Some snake venoms contain polypeptide inhibitors which inactivate mammalian serine-proteinases, including kallikreins, trypsin, plasmin, and a-chymotrypsin (Takahashi et al 1972),. Such proteinase, inhibitors are distributed mainly in the venoms of members of Viperidae and Elapidae (Takahashi et al., 1974a). One of the inhibitors, inhibitor II, isolated from Vipera russelli venom is a polypeptidic substance, consisting of 60 amino acid residues. Its established primary strucutre is very similar to that of the pancreatic basic trypsin inhibitor (Kunitz type) (Takahashi et al., 1974b,c). This report describes the isolation and determination of the amino acid sequence of proteinase inhibitors from the venoms of Hemachatus haemachatus (Ringhals cobra) and Naja nivea (Cape cobra).
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Iwanaga, S., Hokama, Y., Tatsuki, T., Takahashi, H., Suzuki, T. (1976). Isolation and Amino Acid Sequence of Proteinase Inhibitors from the Venoms of Hemachatus haemachatus and Naja nivea . In: Ohsaka, A., Hayashi, K., Sawai, Y., Murata, R., Funatsu, M., Tamiya, N. (eds) Animal, Plant, and Microbial Toxins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-0889-8_4
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DOI: https://doi.org/10.1007/978-1-4684-0889-8_4
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