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- W2109644589 abstract "Abstract The differential pulse polarogram of native liver alcohol dehydrogenase consists of two peaks which correspond to the reduction of zinc associated with the enzyme. On the basis of its electrochemical properties peak I (with peak potential at − 1.0 V) was attributed to the signal of zinc ions liberated from the enzyme adsorbed at the electrode surface. Peak II (with peak potential at − 1.1 V) probably corresponds to the reduction of zinc still bound to the enzyme molecules adsorbed at the electrode surface. The possible difference between the contributions of catalytic and structural zinc of liver alcohol dehydrogenase to the observed currents is discussed. The polarographic behaviour of the enzyme of animal origin is compared with that of yeast alcohol dehydrogenase which yields only one peak at − 1.0 V. The denatured alcohol dehydrogenases give a single signal at −1.0 V which corresponds to the zinc liberated from the enzymes in the solution. The direct denaturation of liver alcohol dehydrogenase in the polarographic cell provides a quick and simple method for determination of the zinc content of the enzyme. In addition, the normal pulse polarograms of native and denatured liver alcohol dehydrogenase show considerable differences." @default.
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- W2109644589 date "1982-07-01" @default.
- W2109644589 modified "2023-10-07" @default.
- W2109644589 title "Polarographic study of zinc bound to alcohol dehydrogenase" @default.
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- W2109644589 doi "https://doi.org/10.1016/0302-4598(82)80023-8" @default.
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