Electron microscopic study of ring-shaped, bivalent hapten, bivalent antidansyl monoclonal antibody complexes with identical variable domains but IgG1, IgG2a and IgG2b constant domains
- 1 February 1990
- journal article
- research article
- Published by Elsevier in Molecular Immunology
- Vol. 27 (2) , 181-190
- https://doi.org/10.1016/0161-5890(90)90113-e
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Computer models of the human immunoglobulins shape and segmental flexibilityImmunology Today, 1986
- Immunoglobulin flexibility in complement activationImmunology Today, 1986
- Immunoglobulin G: Functional sitesMolecular Immunology, 1985
- Correlation between segmental flexibility and effector function of antibodiesNature, 1984
- Quantitative explanation for increased affinity shown by mixtures of monoclonal antibodies: Importance of a circular complexMolecular Immunology, 1983
- Rapid isolation of cloned isotype switch variants using fluorescence activated cell sortingCytometry, 1982
- Segmental flexibility of immunoglobulin G antibody molecules in solution: a new interpretationBiochemistry, 1981
- Multivalent Binding and Functional AffinityPublished by Springer Nature ,1976
- Detection of antibody monomers, dimers and polymers upon interaction of a homologous series of divalent haptens with its specific antibodyBiochemical and Biophysical Research Communications, 1972
- Frictional coefficients of multisubunit structures. II. Application to proteins and virusesBiopolymers, 1967