Quantitative description of the interaction between folate and the folate-binding protein from cow's milk

A detailed study has been carried out on the dependence of folate binding on the concentration of FBP (folate-binding protein) at pH 5.0, conditions selected to prevent complications arising from the pre-existing self-association of the acceptor. In contrast with the mandatory requirement that rever...

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Published inBiochemical journal Vol. 382; no. Pt 1; pp. 215 - 221
Main Authors Nixon, Peter F, Jones, Marc, Winzor, Donald J
Format Journal Article
LanguageEnglish
Published England Portland Press Ltd 15.08.2004
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Abstract A detailed study has been carried out on the dependence of folate binding on the concentration of FBP (folate-binding protein) at pH 5.0, conditions selected to prevent complications arising from the pre-existing self-association of the acceptor. In contrast with the mandatory requirement that reversible interaction of ligand with a single acceptor site should exhibit a unique, rectangular hyperbolic binding curve, results obtained by ultrafiltration for the FBP-folate system required description in terms of (i) a sigmoidal relationship between concentrations of bound and free folate and (ii) an inverse dependence of affinity on FBP concentration. These findings have been attributed to the difficulties in determining the free ligand concentration in the FBP-folate mixtures for which reaction is essentially stoichiometric. This explanation also accounts for the similar published behaviour of the FBP-folate system at neutral pH, which had been attributed erroneously to acceptor self-association, a phenomenon incompatible with the experimental findings because of its prediction of a greater affinity for folate with increasing FBP concentration.
AbstractList A detailed study has been carried out on the dependence of folate binding on the concentration of FBP (folate-binding protein) at pH 5.0, conditions selected to prevent complications arising from the pre-existing self-association of the acceptor. In contrast with the mandatory requirement that reversible interaction of ligand with a single acceptor site should exhibit a unique, rectangular hyperbolic binding curve, results obtained by ultrafiltration for the FBP–folate system required description in terms of (i) a sigmoidal relationship between concentrations of bound and free folate and (ii) an inverse dependence of affinity on FBP concentration. These findings have been attributed to the difficulties in determining the free ligand concentration in the FBP–folate mixtures for which reaction is essentially stoichiometric. This explanation also accounts for the similar published behaviour of the FBP–folate system at neutral pH, which had been attributed erroneously to acceptor self-association, a phenomenon incompatible with the experimental findings because of its prediction of a greater affinity for folate with increasing FBP concentration.
A detailed study has been carried out on the dependence of folate binding on the concentration of FBP (folate-binding protein) at pH 5.0, conditions selected to prevent complications arising from the pre-existing self-association of the acceptor. In contrast with the mandatory requirement that reversible interaction of ligand with a single acceptor site should exhibit a unique, rectangular hyperbolic binding curve, results obtained by ultrafiltration for the FBP-folate system required description in terms of (i) a sigmoidal relationship between concentrations of bound and free folate and (ii) an inverse dependence of affinity on FBP concentration. These findings have been attributed to the difficulties in determining the free ligand concentration in the FBP-folate mixtures for which reaction is essentially stoichiometric. This explanation also accounts for the similar published behaviour of the FBP-folate system at neutral pH, which had been attributed erroneously to acceptor self-association, a phenomenon incompatible with the experimental findings because of its prediction of a greater affinity for folate with increasing FBP concentration.
Author Winzor, Donald J
Nixon, Peter F
Jones, Marc
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Snippet A detailed study has been carried out on the dependence of folate binding on the concentration of FBP (folate-binding protein) at pH 5.0, conditions selected...
A detailed study has been carried out on the dependence of folate binding on the concentration of FBP (folate-binding protein) at pH 5.0, conditions selected...
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StartPage 215
SubjectTerms Animals
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Cattle
Folate Receptors, GPI-Anchored
Folic Acid - metabolism
Hydrogen-Ion Concentration
Milk
Milk Proteins - chemistry
Milk Proteins - metabolism
Molecular Weight
Multiprotein Complexes - chemistry
Protein Binding
Receptors, Cell Surface - chemistry
Receptors, Cell Surface - metabolism
Title Quantitative description of the interaction between folate and the folate-binding protein from cow's milk
URI https://www.ncbi.nlm.nih.gov/pubmed/15142039
https://search.proquest.com/docview/66770209
https://pubmed.ncbi.nlm.nih.gov/PMC1133933
Volume 382
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