Localization of an idiotope on the L chain dimer and intact IgGl immunoglobulin from the patient Mcg
- 1 September 1987
- journal article
- research article
- Published by Elsevier in Molecular Immunology
- Vol. 24 (9) , 937-943
- https://doi.org/10.1016/0161-5890(87)90004-6
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Synthetic peptides corresponding to third hypervariable region of human monoclonal IgM rheumatoid factor heavy chains define an immunodominant idiotype.The Journal of Experimental Medicine, 1985
- Characterization of human rheumatoid factors with seven antiidiotypes induced by synthetic hypervariable region peptides.The Journal of Experimental Medicine, 1985
- Unexpected similarities in the crystal structures of the Mcg light-chain dimer and its hybrid with the weir proteinMolecular Immunology, 1985
- A search for site-filling ligands in the Mcg bence-jones dimer: Crystal binding studies of fluorescent compoundsMolecular Immunology, 1984
- Rapid and sensitive procedure for assigning idiotypic determinants to heavy or light chains: Application to idiotopes associated with the major cross-reactive idiotype of A/J anti-phenylarsonate antibodiesMolecular Immunology, 1983
- Primary structure of a human λ-chain (Weir) of the Mcg typeMolecular Immunology, 1982
- Rotational allomerism and divergent evolution of domains in immunoglobulin light chainsBiochemistry, 1975
- Primary structure of the Mcg λ chainBiochemistry, 1974
- Amino acid sequence of κ Bence Jones protein from a case of primary amyloidosisBiochemistry, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970