The ligand binding and aggregation behavior of cow's milk folate binding protein depends on hydrogen ion concentration and buffer composition. At pH 5.0, the protein polymerizes in Tris-HCl subsequent to ligand binding. No polymerization occurs in acetate, and binding is markedly weaker in acetate or citrate buffers as compared to Tris-HCl. Polymerization of ligand-bound protein was far more pronounced at pH 7.4 as compared to pH 5.0 regardless of buffer composition. Binding affinity increased with decreasing concentration of protein both at pH 7.4 and 5.0. At pH 5.0 this effect seemed to level off at a protein concentration of 10−6 M which is 100–1000 fold higher than at pH 7.4. The data can be interpreted in terms of complex models for ligand binding systems polymerizing both in the absence or presence of ligand (pH 7.4) as well as only subsequent to ligand binding (pH 5.0).
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Research Article|
December 01 2001
Effect of Hydrogen Ion Concentration and Buffer Composition on Ligand Binding Characteristics and Polymerization of Cow's Milk Folate Binding Protein
Jan Holm;
Jan Holm
1Department of Clinical Chemistry, Central Hospital Bornholm, Roenne, DK-3700, Denmark
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Steen Ingemann Hansen
Steen Ingemann Hansen
2Department of Clinical Chemistry, Central Hospital, Hollerød, DK-3400, Denmark
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Publisher: Portland Press Ltd
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 2001 Plenum Publishing Corporation
2001
Biosci Rep (2001) 21 (6): 745–753.
Citation
Jan Holm, Steen Ingemann Hansen; Effect of Hydrogen Ion Concentration and Buffer Composition on Ligand Binding Characteristics and Polymerization of Cow's Milk Folate Binding Protein. Biosci Rep 1 December 2001; 21 (6): 745–753. doi: https://doi.org/10.1023/A:1015528606487
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