The effects of cleavage of the inter-chain disulphide bonds of rabbit IgG on its ability to bind C1q
- 1 May 1984
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 787 (1) , 39-44
- https://doi.org/10.1016/0167-4838(84)90105-5
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Formation of complement subcomponent C1q-immunoglobulin G complex. Thermodynamic and chemical-modification studiesBiochemical Journal, 1982
- Effect of reduction and alkylation on structure and function of rabbit IgG antibody—I. Effect on ability to activate complement depends on conditions of reductionMolecular Immunology, 1981
- Conversion of the reactive sulfhydryl groups of proteins to the S-trifluoroethyl derivativesAnalytical Biochemistry, 1981
- Activation of the Complement System by Antibody-Antigen Complexes: The Classical PathwayAdvances in Protein Chemistry, 1979
- Interaction of human Clq with insoluble immunoglobulin aggregatesImmunochemistry, 1978
- The role of the inter-heavy chain disulfide bond in modulating the flexibility of immunoglobulin G antibodyJournal of Molecular Biology, 1977
- Structure and function of the constant regions of immunoglobulinsQuarterly Reviews of Biophysics, 1976
- Characterization of a plasmin-digest fragment of rabbit immunoglobulin gamma that binds antigen and complementBiochemical Journal, 1975
- Synthesis and characterization of two fluorescent sulfhydryl reagentsBiochemistry, 1973
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971