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• W2084262011 abstract "The association rate constant for the binding of bilirubin to bovine serum albumin has been determined in a continuous-flow experiment. The value obtained is 0.9 x 106m−1S−1. Furthermore the dissociation rate constant is determined from the rate of the peroxidase-catalyzed oxidation of bilirubin in a bilirubin-albumin solution. This figure is 3.1 × 10−2s 1. Calculation of the apparent binding equilibrium constant from the two rate constants gives 2.9 x 107m−1. The above mentioned peroxidase oxidation has also been used for a direct estimation of the binding equilibrium constant giving 2.7 × 107m−1. All experiments are carried out at 36 °C and pH 7.4." @default.
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• W2084262011 date "1975-06-01" @default.
• W2084262011 modified "2023-10-17" @default.
• W2084262011 title "Determination of association and dissociation rate constants for bilirubin-bovine serum albumin" @default.
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• W2084262011 doi "https://doi.org/10.1016/0003-9861(75)90263-5" @default.
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