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STRUCTURE AND SPECIFICITY OF GUINEA PIG 7S ANTIBODIES
Additional evidence has been obtained to show that different guinea pig anti-hapten antibodies differ in the structure of their L polypeptide chains. Antibodies from animals immunized with the same hapten conjugated to different carrier proteins gave similar starch gel electrophoretic patterns after dissociation of their chains. In a study of fine differences of specificity, cross-reacting antibodies were found to have some L chains with the same electrophoretic mobility. The multiplicity of L chain bands found in the characteristic starch gel electrophoretic patterns of dissociated anti-DNP antibodies was shown to be a reflection of the heterogeneity of antibodies of slightly different specificities. Reduction and alkylation of the active fragment produced by digestion of antibodies with papain yielded starch gel electrophoretic bands corresponding in mobility to L chains. The results are consistent with the notion that L chains are involved in the acquisition of immunologic specificity.
Additional evidence has been obtained to show that different guinea pig anti-hapten antibodies differ in the structure of their L polypeptide chains. Antibodies from animals immunized with the same hapten conjugated to different carrier proteins gave similar starch gel electrophoretic patterns after dissociation of their chains. In a study of fine differences of specificity, cross-reacting antibodies were found to have some L chains with the same electrophoretic mobility. The multiplicity of L chain bands found in the characteristic starch gel electrophoretic patterns of dissociated anti-DNP antibodies was shown to be a reflection of the heterogeneity of antibodies of slightly different specificities. Reduction and alkylation of the active fragment produced by digestion of antibodies with papain yielded starch gel electrophoretic bands corresponding in mobility to L chains. The results are consistent with the notion that L chains are involved in the acquisition of immunologic specificity.
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01:10Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
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The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.