Journal article
Antibody-directed liposomes Determination of affinity constants for soluble and liposome-bound antifluorescein
Biochimica et biophysica acta. Biomembranes, v 770(2), 148
14 Mar 1984
PMID: 6421325
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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.
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Details
- Title
- Antibody-directed liposomes Determination of affinity constants for soluble and liposome-bound antifluorescein
- Creators
- T.D. Heath - Cancer Research InstituteR.T. Fraley - Cancer Research InstituteJ. Bentz - University of California, San FranciscoVoss E.W. - Department of Microbiology, University of Illinois, Champaign Urbana, IL 61801 U.S.AJ.N. Herron - University of Illinois Urbana-ChampaignD. Papahadjopoulos - Cancer Research Institute
- Publication Details
- Biochimica et biophysica acta. Biomembranes, v 770(2), 148
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:A1984SK60400007
- Scopus ID
- 2-s2.0-0021762085
- Other Identifier
- 991021463708204721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics