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 1 1986 |
| Externally published | Yes |
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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
Cite this
Further studies on the interaction of immobilized folate binding protein and enzyme-folate conjugates; an enzyme-linked competitive binding assay for folate. / Bachas, Leonidas G; Ashcom, G. S.; Meyerhoff, M. E.
In: Analytical Letters, Vol. 19, No. 15-16, 01.01.1986, p. 1653-1678.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Further studies on the interaction of immobilized folate binding protein and enzyme-folate conjugates; an enzyme-linked competitive binding assay for folate
AU - Bachas, Leonidas G
AU - Ashcom, G. S.
AU - Meyerhoff, M. E.
PY - 1986/1/1
Y1 - 1986/1/1
N2 - 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.
AB - 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.
KW - competitive binding assay enzyme cooperativity infant formula
KW - folic acid folate binding protein
UR - http://www.scopus.com/inward/record.url?scp=84912719413&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84912719413&partnerID=8YFLogxK
U2 - 10.1080/00032718608066313
DO - 10.1080/00032718608066313
M3 - Article
AN - SCOPUS:84912719413
VL - 19
SP - 1653
EP - 1678
JO - Analytical Letters
JF - Analytical Letters
SN - 0003-2719
IS - 15-16
ER -