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- W984042887 abstract "Publisher Summary This chapter reviews less used spectrophotometric titrations and reconsiders older uses, in particular the interpretation of titration curves obtained at high pH. A spectrophotometric titration of a protein is usually understood as the titration of its phenolic groups by measurement of the change in absorption at 295nm. A spectrophotometric titration can be carried out whenever the dissociation of a proton results in a change in the spectrum of one or more chromophores. If the dissociating group is not actually a chromophore, it must interact with some chromophore so that proton dissociation results in a change in the spectrum of the protein. The dissociation constants of metal ions or any ion or molecule bound to a protein, which produces a change in spectrum can be obtained in the same manner. As spectral changes are often small, a reference solution of similar absorption properties is normally used and measurements are obtained as differences from this reference solution." @default.
- W984042887 created "2016-06-24" @default.
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- W984042887 date "1973-01-01" @default.
- W984042887 modified "2023-10-15" @default.
- W984042887 title "[22] Spectrophotometric titration of the functional groups of proteins" @default.
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- W984042887 doi "https://doi.org/10.1016/s0076-6879(73)27025-8" @default.
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