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) |
|---|---|
| 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
Fingerprint Dive into the research topics of 'Further studies on the interaction of immobilized folate binding protein and enzyme-folate conjugates; an enzyme-linked competitive binding assay for folate'. Together they form a unique fingerprint.
Cite this
Bachas, L. G., Ashcom, G. S., & Meyerhoff, M. E. (1986). Further studies on the interaction of immobilized folate binding protein and enzyme-folate conjugates; an enzyme-linked competitive binding assay for folate. Analytical Letters, 19(15-16), 1653-1678. https://doi.org/10.1080/00032718608066313