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

Evaluation of fluorescence polarization method for binding study in carbohydrate-lectin interaction

Y Oda1, M Kinoshita, K Nakayama

  • 1Faculty of Pharmaceutical Sciences, Kinki University, Higashi-osaka, Japan.

Biological & Pharmaceutical Bulletin
|December 16, 1998
PubMed
Summary

Fluorescence polarization (FP) effectively detects molecular interactions between plant lectins and various biomolecules. This sensitive method quantifies interactions without washing, simplifying biological assays.

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

Bovine κ-casein inhibits human rotavirus (HRV) infection via direct binding of glycans to HRV.

Journal of dairy science·2014
Same author

[Mechanical environment during parabolic flight of MU-300 jet plane].

Uchu Seibutsu Kagaku·2003
Same author

Specific distribution of sialic acids in animal tissues as examined by LC-ESI-MS after derivatization with 1,2-diamino-4,5-methylenedioxybenzene.

Analytical chemistry·2002
Same author

Fluorescence polarization: analysis of carbohydrate-protein interaction.

Analytical biochemistry·2001
Same author

Anomalous migration of hyaluronic acid oligomers in capillary electrophoresis: correlation to susceptibility to hyaluronidase.

Electrophoresis·2001
Same author

Lactone formation of N-acetylneuraminic acid oligomers and polymers as examined by capillary electrophoresis.

Electrophoresis·2001

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Plant lectins are proteins that bind carbohydrates.
  • Understanding lectin-carbohydrate interactions is crucial in biology and medicine.
  • Fluorescence polarization (FP) is a biophysical technique used to study molecular interactions.

Purpose of the Study:

  • To evaluate the fluorescence polarization (FP) technique for determining molecular interactions.
  • To assess the binding of plant lectins to polysaccharides, yeast cells, and glycopeptides.
  • To demonstrate the utility of FP in quantitative analysis of biomolecular interactions.

Main Methods:

  • Plant lectins, including Lycoris radiata agglutinin, were labeled with fluorescein isothiocyanate.
  • Fluorescence polarization measurements were performed to detect binding events.

Related Experiment Videos

  • The FP method was applied to interactions with mannose-containing biomolecules and a fluorescein-labeled glycopeptide.
  • Main Results:

    • The FP technique successfully determined molecular interactions between labeled plant lectins and polysaccharides.
    • Lycoris radiata agglutinin binding to mannose-containing biomolecules was quantifiable using FP.
    • FP analysis of a fluorescein-labeled glycopeptide demonstrated its effectiveness for quantitative interaction studies.
    • The FP method proved to be highly sensitive and did not require washing steps.

    Conclusions:

    • Fluorescence polarization is a sensitive and facile method for studying molecular interactions involving plant lectins.
    • The FP technique allows for quantitative assessment of binding between lectins and various carbohydrate structures.
    • This method offers a simplified approach to analyzing biomolecular interactions without the need for washing procedures.