The circular dichroism of phosphocholine-specific mouse hybridoma and myeloma proteins: Unusual properties of the hybridoma protein 101.6g6
- 1 March 1985
- journal article
- research article
- Published by Elsevier in Molecular Immunology
- Vol. 22 (3) , 305-311
- https://doi.org/10.1016/0161-5890(85)90166-x
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- The role of a novel VH sequence (V11) in the formation of anti-phosphocholine antibodiesMolecular Immunology, 1984
- Anti-phosphocholine hybridoma antibodies. II. Functional analysis of binding sites within three antibody families.The Journal of Experimental Medicine, 1981
- Possible three-dimensional backbone folding around antibody combining site of immunoglobulin MOPC167Journal of Theoretical Biology, 1981
- A hypothetical space-filling model of the V-regions of the galactan-binding myeloma immunoglobulin J539☆Molecular Immunology, 1981
- Anti-phosphocholine hybridoma antibodies. I. Direct evidence for three distinct families of antibodies in the murine responseThe Journal of Experimental Medicine, 1981
- Structural basis for the specificity of phosphorylcholine-binding immunoglobulinsImmunochemistry, 1976
- Comparison of three phosphorylcholine-binding mouse myeloma proteins by circular dichroismBiochemical and Biophysical Research Communications, 1974
- Use of dextran conjugated columns for the isolation of large quantities of MOPC 104E IgMImmunochemistry, 1972
- Immunochemical studies on mouse myeloma proteins with specificity for dextran or for levanImmunochemistry, 1972
- Specificity for phosphorylchloine of six murine myeloma proteins reactive with Pneumococcus C polysaccharide and β-lipoproteinBiochemistry, 1971