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- W2003188631 abstract "The complex formation between pyridoxal 5′-phosphate (PLP) and bovine serum albumin at pH=7.0 and 25 °C was characterized by four relaxation processes. The dependence of the reciprocal relaxation times upon reactant concentrations was found to be consistent with a mechanism in which a rapid bimolecular binding step is followed by three sequential isomerization steps. The eight rate constants for this mechanism were determined and then combined to calculate an overall equilibrium constant which is in agreement with the literature value. Absorption spectra of the complexes formed by the two faster steps were determined from absorbance changes associated with them; the spectrum corresponding to the first complex has two bands at 330 nm and 360 nm and an additional 410 nm band, while the spectrum corresponding to the second complex has a large single band at 375 nm. Comparing these spectra with those reported for other PLP-enzyme systems, we speculate that four steps in the proposed mechanism may correspond t..." @default.
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- W2003188631 date "1986-11-01" @default.
- W2003188631 modified "2023-09-25" @default.
- W2003188631 title "Stopped-Flow Kinetic Study of the Complex Formation between Pyridoxal 5′-Phosphate and Bovine Serum Albumin" @default.
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- W2003188631 doi "https://doi.org/10.1246/bcsj.59.3399" @default.
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