Further studies on the interaction of immobilized folate binding protein and enzyme-folate conjugates; an enzyme-linked competitive binding assay for folate

L. G. Bachas; G. S. Ashcom; M. E. Meyerhoff

doi:10.1080/00032718608066313

Further studies on the interaction of immobilized folate binding protein and enzyme-folate conjugates; an enzyme-linked competitive binding assay for folate

L. G. Bachas, G. S. Ashcom, M. E. Meyerhoff

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

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	https://doi.org/10.1080/00032718608066313
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

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title = "Further studies on the interaction of immobilized folate binding protein and enzyme-folate conjugates; an enzyme-linked competitive binding assay for folate",

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.",

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author = "Bachas, {L. G.} and Ashcom, {G. S.} and Meyerhoff, {M. E.}",

note = "Funding Information: ACKNOWLEDGEMENTS We gratefully acknowledge the National Science Foundation for supporting this work (Grant # CHE-8506695). We also wish to thank the Program in Scholarly Research for Urban/Minor ity High School Students for their support. Copyright: Copyright 2016 Elsevier B.V., All rights reserved.",

year = "1986",

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doi = "10.1080/00032718608066313",

language = "English (US)",

volume = "19",

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journal = "Analytical Letters",

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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, L. G.

AU - Ashcom, G. S.

AU - Meyerhoff, M. E.

N1 - Funding Information: ACKNOWLEDGEMENTS We gratefully acknowledge the National Science Foundation for supporting this work (Grant # CHE-8506695). We also wish to thank the Program in Scholarly Research for Urban/Minor ity High School Students for their support. Copyright: Copyright 2016 Elsevier B.V., All rights reserved.

PY - 1986/1

Y1 - 1986/1

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.

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Further studies on the interaction of immobilized folate binding protein and enzyme-folate conjugates; an enzyme-linked competitive binding assay for folate

Abstract

Keywords

ASJC Scopus subject areas

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