Abstract
The reaction product of uranyl nitrate with whole-protein Bushmaster snake venom in nitrate buffer at pH 3.5 has been studied. The maximum uptake of uranium was 291 μmol U·g−1 of venom. The infrared spectrum of the product showed an asymmetric O−U−O vibration at 921 cm−1 typical of complex formation with the uranyl ion. Stability measurements with the UO 2+2 -protein complex in neutral medium indicated moderate hydrolytic stability, with 14% dissociation after 16 hours at 0°C. Neutron irradiation and desorption studies with a235U-labelled complex showed that generated fission products such as lanthanides and barium were readily lixiviated at pH 7, whereas Ru and Zr were highly retained by the protein substrate.
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MacCordick, H.J., Taghva, F., Meyer, J.P. et al. Interaction of uranyl ions with snake venom proteins fromLachesis muta muta . J Radioanal Nucl Chem 223, 187–191 (1997). https://doi.org/10.1007/BF02223382
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DOI: https://doi.org/10.1007/BF02223382