1. Biochemical characterization of surface immunoglobulin
- Author
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Higgins G, Lifter J, and Yong Sung Choi
- Subjects
Glycosylation ,Surface Immunoglobulin ,Detergents ,Plasma Cells ,Immunology ,Receptors, Antigen, B-Cell ,Centrifugation, Isopycnic ,Plasma cell ,chemistry.chemical_compound ,medicine ,Animals ,Humans ,Molecule ,Molecular Biology ,Integral membrane protein ,Differential centrifugation ,B-Lymphocytes ,biology ,Electrophoresis ,medicine.anatomical_structure ,chemistry ,Biochemistry ,Immunoglobulin G ,biology.protein ,Electrophoresis, Polyacrylamide Gel ,Antibody ,Chickens - Abstract
Charge-shift electrophoresis and isopycnic centrifugation were used to investigate the binding of detergents by B-cell and plasma cell immunoglobulin. Plasma cell immunoglobulin did not bind detergent; neither its electrophoretic migration nor buoyant density were altered by the presence of detergents. In contrast, B-cell immunoglobulin bound detergent, which resulted in a change in electrophoretic behavior and a reduced buoyant density in CsCI gradients. At least 20–23 molecules of Triton X-100 were bound by each molecule of B-cell immunoglobulin. With respect to detergent binding, B-cell immunoglobulin was similar to other hydrophobic integral membrane proteins. Since detergent binding was unaffected by the extent of glycosylation of the molecule, the hydrophobicity of B-cell immunoglobulin was most likely due to the chemical nature of the polypeptide chain. The approximate molecular weight of the heavy chain of surface IgG is 77,000 which is larger than that of secreted IgG with molecular weight of 67,000. The Fc portion of the immunoglobulin molecule is proposed as the most probable location for the site of detergent binding.
- Published
- 1980
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