Abstract
The kinetic and thermodynamic properties of the folate interaction with immobilized folate binding protein (FBP) are examined. The use of enzyme- rather than radio-labeled folate provides insight into the complex binding mechanism of folate with FBP and indicates that polymerization of the binding protein (evident for FBP-folate association in solution) is not a prerequisite for the cooperative behavior observed. An enzyme-linked competitive binding assay for folate based on this interaction is described and dose-response curves demonstrate the sensitivity and selectivity of the method. The accuracy of the assay is tested by determining folate in infant formula.
Original language | English (US) |
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Pages (from-to) | 1653-1678 |
Number of pages | 26 |
Journal | Analytical Letters |
Volume | 19 |
Issue number | 15-16 |
DOIs | |
State | Published - Jan 1986 |
Externally published | Yes |
Keywords
- competitive binding assay enzyme cooperativity infant formula
- folic acid folate binding protein
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry
- Spectroscopy
- Clinical Biochemistry
- Biochemistry, medical
- Electrochemistry