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- W2023985286 abstract "Functional differences in high- and low-temperature conformations of monomers and dimers of d-amino acid oxidase (holoenzyme) were studied by the kinetic method. No difference was found in oxidase activity between the high- and low-temperature conformations. However, the specific rate constant of the monomer was about 5 times greater than that of the dimer. The apparent dimerization constant (K), was determined at various temperatures, pH levels and concentrations of NaCl by the kinetic method. As the temperature was lowered, values of K decreased and in the temperature range between 19 and 15°, a sharp transition of K values was observed. As pH level decreased and the concentration of NaCl increased, values of K decreased." @default.
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- W2023985286 date "1972-04-01" @default.
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- W2023985286 title "The kinetic features of monomers and dimers in high- and low-temperature conformational states of d-amino acid oxidase" @default.
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- W2023985286 doi "https://doi.org/10.1016/0005-2795(72)90082-7" @default.
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