These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The interaction between wheat germ agglutinin and membrane incorporated glycophorin A. An optical binding study.
    Author: Ramsden JJ, Wright CS.
    Journal: Glycoconj J; 1995 Apr; 12(2):113-21. PubMed ID: 7620327.
    Abstract:
    A novel integrated optical technique is used to monitor the kinetics of incorporation of glycophorin A (GPA) from solution into a planar dimyristoylphosphatidylcholine-cholesterol bilayer membrane, and the subsequent binding of wheat germ agglutinin (WGA) to the membrane-incorporated GPA. The technique significantly improves the attainable accuracy of kinetic measurements. The number of bound molecules can be determined to a precision of ca +/- 80 mol microns-2. Our results show that GPA incorporates spontaneously into the bilayer. Binding of WGA to GPA is optimal in the presence of human serum albumin, and can be reversed by N-acetyl-D-glucosamine. The kinetics of the binding are consistent with the presence of two classes of kinetically distinguishable binding sites with association rates of 2.0 x 10(4) and 9.6 x 10(2) M-1 s-1, and dissociation rates of 2.7 x 10(-3) s-1 and < 10(-5) s-1, respectively. A stoichiometry of 4 WGA monomers per GPA monomer was determined as characteristic of the overall binding interaction.
    [Abstract] [Full Text] [Related] [New Search]