Logo image
Antibody-directed liposomes Determination of affinity constants for soluble and liposome-bound antifluorescein
Journal article   Peer reviewed

Antibody-directed liposomes Determination of affinity constants for soluble and liposome-bound antifluorescein

T.D. Heath, R.T. Fraley, J. Bentz, Voss E.W., J.N. Herron and D. Papahadjopoulos
Biochimica et biophysica acta. Biomembranes, v 770(2), 148
14 Mar 1984
PMID: 6421325

Abstract

Antibody conjugate Antigen binding Fluorescein Fluorescence quenching Human erythrocyte Liposome Liposome-cell interaction
We have used the binding of liposomes conjugated with antifluorescein antibody specific for fluorescein isothiocyanate-modified erythrocytes as a model for multivalent antigen-antibody interactions. We examined a series of liposome preparations which were conjugated to between 0 and 332 active antibodies per liposome. The antigen binding capacity and mean intrinsic affinity of the soluble and conjugated antibody were determined by fluorescence quenching of carboxyfluorescein. Liposome-cell interaction data were fitted with a Scatchard-type equation. Functional affinity of liposomes for cells was up to 1000-fold greater than the intrinsic affinity of the antibody for soluble ligand. Analysis for binding at high cell concentrations revealed that liposome-induced cell agglutination reduces the number of available binding sites per cell.

Metrics

5 Record Views
34 citations in Scopus

Details

UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

InCites Highlights

Data related to this publication, from InCites Benchmarking & Analytics tool:

Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Biophysics
Logo image