Journal article
Antibody-directed liposomes. Determinaion of affinity constants for soluble and liposome-bound antifluorescein
Biochimica et biophysica acta, Protein structure and molecular enzymology, Vol.770(2)
01 Jan 1984
Abstract
The authors have used the binding of liposomes conjugated with antifluorescein antibody specific for fluorescein isothiocyanate-modified erythrocytes as a model for mutlivalent antigen-antibody interactions. A series of liposome preparations which were conjugated to between 0 and 332 active antibodies per liposome were examined. 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 100-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
1 Record Views
Details
- Title
- Antibody-directed liposomes. Determinaion of affinity constants for soluble and liposome-bound antifluorescein
- Creators
- T HeathR FraleyJ BentzE W VossJ HerronD Papahadjopoulos
- Publication Details
- Biochimica et biophysica acta, Protein structure and molecular enzymology, Vol.770(2)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Identifiers
- 991021463435104721