Abstract
The carbohydrate chains on the light chains of human antibody HB4C5 reactive to human lung adenocarcinoma tissue have been characterized. Human hybridoma HB4C5 produced antibody consists with two kinds of light chains with different carbohydrate chains (hybrid and complex types, respectivery) linked to the variable regions. The light chain with hybrid-type has been comfirmed to be active species for antibody binding to lung cancer tissue. Concanavalin A-resistants of this cell line and of its subline C5TN, produced variant antibodies consisted with light chains with altered carbohydrate chains. The variant-antibodies showed altered antigen binding specificity and affinity. Futhermore, several glycosidase treatment to the variant-antibodies changed the antigen binding. These results indicate that the presence and the structure of carbohydrate chain is critical for antigen binding of the antibody.
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