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- W1520762712 abstract "The simple sequential model P1 + Pi ag P1 + i, i = 1, 2, …, ∞K1 = K2 = …. = Ki = P1P̄iP̄1+i, which quantitatively rationalizes liver glutamate dehydrogenase molecular weight data (Reisler & Eisenberg, 1971; Sund et al., 1972; Malencik & Anderson, 1972; Chun et ed., 1972) is subjected to a rigorous kinetic analysis. With the reasonable assumption that all elementary steps are characterized by identical rate constants, the relaxation times and corresponding scattered light relaxation amplitudes are computed for the above scheme as a function of concentration, and presented in a general form applicable to an arbitrary open polymerization. When related to the glutamate dehydrogenase system, the kinetic analysis predicts that first-order plots of changes in scattered light intensity should be non-linear above about 1 mg/ml. In general, the half-life of the overall decay should increase with total solute concentration. These predictions are incompatible with the highly degenerate nature of the observed relaxation spectrum and the monotonic decrease of the experimental relaxation time with concentration (Fisher & Bard, 1969; Kempfle & Winkler, 1973; Thusius et al., 1975). The discrepency between the predicted and observed kinetic behaviour leads to the exclusion of the sequential model and strongly suggests that monomer does not play a critical role in the spontaneous self-assembly. Rather, all kinetic and equilibrium results available to date are consistent with condensations occurring between all species without discrimination (Thusius et al., 1975). The glutamate dehydrogenase system apparently represents the extreme case of a linear aggregation proceeding via polymers possessing identical and independent association sites." @default.
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- W1520762712 date "1975-05-01" @default.
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- W1520762712 title "Mechanism of bovine liver glutamate dehydrogenase self-assembly" @default.
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- W1520762712 doi "https://doi.org/10.1016/0022-2836(75)90208-9" @default.
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