Equilibrium and Kinetic Studies of the Interaction between Orange I and Bovine Serum Albumin
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Link
https://www.jstage.jst.go.jp/article/bcsj1926/61/4/61_4_1323/_pdf
Reference23 articles.
1. Heterogeneity of the Binding Sites of Bovine Serum Albumin1
2. Kinetics of the binding of bilirubin to human serum albumin studied by stopped-flow technique
3. Kinetics and mechanism of bilirubin binding to human serum albumin.
4. The rate of access to the organic ligand-binding region of serum albumin is entropy controlled.
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1. Interaction of a reactive dye with serum albumins and with aminoacids: the dye as a chiral label;Dyes and Pigments;2002-12
2. Resolution of the Absorbance and CD Spectra and Formation Constants of the Complexes between Human Serum Albumin and Methyl Orange;Chemistry - A European Journal;1996-02
3. A Structure-Activity Relationship in the Binding of Multicharged Anionic Azo and Pyrene Dyes to Serum Albumin;Bulletin of the Chemical Society of Japan;1994-10
4. Equilibrium and Kinetic Studies of the Binding of Monoanionic and Dianionic Ligands to Bovine Serum Albumin;Bulletin of the Chemical Society of Japan;1993-10
5. Equilibrium and kinetic studies of the binding of tri- and tetra-anionic ligands to bovine serum albumin;Biophysical Chemistry;1991-12
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