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Updated: Oct 21, 2026

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
Published on: June 29, 2016
A bovine epithelial membrane protein that binds polymeric immunoglobulin and has a structure related to that of
Abstract:
A protein of Mr 94000 was isolated from detergent-solubilized bovine intestinal, liver and mammary-gland membranes. It binds immunoglobulin M and also undergoes proteolytic fragmentation in a similar manner to bovine secretory component (Mr 74000). The affinity-purified membrane protein is therefore most likely to be the bovine epithelial receptor for polymeric immunoglobulin. A structural model is proposed.
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Antibody 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 consist of four polypeptide chains: two identical heavy...
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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.
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