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 journalArticle

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 languageEnglish (US)
Pages (from-to)1653-1678
Number of pages26
JournalAnalytical Letters
Volume19
Issue number15-16
DOIs
StatePublished - Jan 1986
Externally publishedYes

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