Covalent Immunoglobulin Assembly in Vitro: Reactivity of Light Chain Covalent Dimers (L 2 ) and Blocked Light Chain Monomers
- 10 February 1978
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 199 (4329) , 688-690
- https://doi.org/10.1126/science.415360
Abstract
Covalent light chain dimers (L2) and cysteine-blocked L chain monomers readily react with partially reduced heavy (H) chains. A rapid disappearance of these blocked L chain species is followed by the appearance of covalent intermediates-HL, H2, and H2L-leading to fully assembled H2L2. The mechanism of initial disulfide bond formation between heavy and light chains is disulfide interchange.Keywords
This publication has 11 references indexed in Scilit:
- Acquisition of the covalent quaternary structure of an immunoglobulin G molecule. Reoxidative assembly in vitroBiochemistry, 1977
- Relative susceptibilities of the interchain disulfides of an immunoglobulin G molecule to reduction by dithiothreitolBiochemistry, 1977
- Synthesis, Assembly and Secretion of γ-Globulin by Mouse Myeloma CellsThe Journal of Immunology, 1973
- Acquisition of Three-Dimensional Structure of ProteinsAnnual Review of Biochemistry, 1973
- The Unique Reassociation of Human IgA2 Immunoglobulins from Dimer SubunitsThe Journal of Immunology, 1972
- Biosynthesis of immunoglobulinsProgress in Biophysics and Molecular Biology, 1972
- The recombination of dimers of immunoglobulin peptide chainsBiochemical Journal, 1970
- Biosynthesis and Assembly of Immunoglobulin GCold Spring Harbor Symposia on Quantitative Biology, 1967
- Synthesis of Excess Light Chains of Gamma Globulin by Rabbit Lymph Node CellsNature, 1966
- PROTEIN-PROTEIN INTERACTIONS AMONG L POLYPEPTIDE CHAINS OF BENCE-JONES PROTEINS AND HUMAN γ-GLOBULINSThe Journal of Experimental Medicine, 1964