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- W2071435309 abstract "Abstract The mussels, Mytilus galloprovincialis, were exposed for 22 days to 230 μg Cd dm−3. Crude homogenate was untreated and thermally treated at 70°C for 10 min. Supernatant of 27,000 g was fractionated on a Sephadex G-75 column at + 4°C. Five fractions from the metallothionein-like-proteins (MLPs) group, containing different concentrations of cadmium- and sulphur-containing proteins, were selected and investigated for cadmium complexing capacity by titration with increasing cadmium concentrations, at pH 1.3 and 8.5. In isolated proteins from both untreated and thermally treated homogenates, two types of binding sites were recorded at 25°C and 0.7 M ionic strength. The first, strong binding site L1 is available at an average cadmium concentration of 1.1 x 10−7 mol dm−3. The average stability constant K1 of the CdL2 complex is 1.7 x 108 dm3 mol−1. The second, weaker binding site L2 is available at an average cadmium concentration of 2.2 x 10−7 mol dm−3, and average stability constant K2 of the complex CdL2 is 2 x 108 dm3 mol−1. Based on the stepwise stability constants K1 and K2, the overall stability constant β2 has been calculated as 3 x 1014 (dm3, mol1)−2." @default.
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- W2071435309 date "1989-12-01" @default.
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- W2071435309 title "Cadmium-induced proteins from mytilus galloprovincialis - polarographic characterization and study of their interaction with cadmium" @default.
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- W2071435309 doi "https://doi.org/10.1016/0304-4203(89)90195-3" @default.
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