Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Solid phase enzyme-linked competitive binding assay for riboflavin.

G S Cha1, M E Meyerhoff

  • 1Department of Chemistry, University of Michigan, Ann Arbor 48109.

Analytical Biochemistry
|January 1, 1988
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Enhancing analytical accuracy of intravascular electrochemical oxygen sensors via nitric oxide release using S-nitroso-N-acetyl-penicillamine (SNAP) impregnated catheter tubing.

Talanta·2019
Same author

Pep19 drives epitope spreading in periodontitis and periodontitis-associated autoimmune diseases.

Journal of periodontal research·2015
Same author

Potentiometric properties of ion-selective electrode membranes based on segmented polyether urethane matrices.

Analytical chemistry·2011
Same author

One-component room temperature vulcanizing-type silicone rubber-based calcium-selective electrodes.

Analytical chemistry·2011
Same author

Enhanced Serum Carbon Dioxide Measurements with a Silicone Rubber-Based Carbonate Ion-Selective Electrode and a High-pH Dilution Buffer.

Analytical chemistry·2011
Same author

Disposable amperometric glucose sensor electrode with enzyme-immobilized nitrocellulose strip.

Talanta·2008
Same journal

Lysozyme assay using a rationally designed GN4G2 substrate with coupled β-glucosidase reaction.

Analytical biochemistry·2026
Same journal

The long run: A tribute to Arthur Joseph Lawrence Cooper.

Analytical biochemistry·2026
Same journal

Evaluation of a method for affinity measurement using solution equilibrium titration with magnetic beads.

Analytical biochemistry·2026
Same journal

Metabolomics approach using UHPLC/QE-MS for the mechanism of He Xue Ming Mu tablets on non-proliferative diabetic retinopathy.

Analytical biochemistry·2026
Same journal

UniRES-GO: Unified residue-level early fusion of sequence and predicted structure for protein function prediction.

Analytical biochemistry·2026
Same journal

IgG detection by enzyme-linked mass spectrometric assay versus color, fluorescent, ECL in buffer and serum.

Analytical biochemistry·2026
See all related articles

A new enzyme-linked assay accurately measures riboflavin (vitamin B2) using a competitive binding method. This method optimizes enzyme conjugate activity for reliable detection in various samples like urine and infant formula.

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Enzyme Assays

Background:

  • Riboflavin (vitamin B2) is essential, requiring accurate quantification.
  • Existing methods for riboflavin analysis may lack sensitivity or selectivity.
  • Development of a robust, solid-phase assay is needed for diverse sample matrices.

Purpose of the Study:

  • To develop and validate a novel solid-phase enzyme-linked assay for quantifying riboflavin.
  • To optimize assay parameters for enhanced sensitivity and detection limits.
  • To assess the assay's applicability for direct riboflavin measurement in biological and food samples.

Main Methods:

  • A competitive solid-phase enzyme-linked immunoassay format was established.
  • The assay utilizes a glucose-6-phosphate dehydrogenase-3-carboxymethylriboflavin conjugate and riboflavin-binding protein immobilized on Sepharose.

Related Experiment Videos

  • Reaction conditions (pH, solvent) for conjugate preparation were optimized to improve enzyme activity and detectability.

    • Main Results:

    • Optimized reaction conditions significantly enhanced conjugate catalytic activity and assay detectability.
    • Assay performance, including detection limits and dose-response sensitivity, was optimized by adjusting the ratio of conjugate to binding sites.
    • The assay demonstrated good selectivity, correlating with known binding affinities, and adequate performance for riboflavin measurement in urine, infant formula, and vitamin capsules.

    Conclusions:

    • A novel, optimized solid-phase enzyme-linked assay provides sensitive and selective riboflavin quantification.
    • The assay is suitable for direct measurement of riboflavin in complex matrices such as urine, infant formula, and vitamin supplements.
    • This method offers a valuable tool for nutritional monitoring and quality control applications.