Immunoglobulins, glycosylation

Dissolve the antibody to be labeled in 0.1 M sodium phosphate, 0.15 M NaCl, pH 7.5, at a concentration of at least lOmg/ml. The immunoglobulin must be glycosylated to work in this procedure. 

Endo, T., Wright, A., Morrison, S.L., and Kobata, A. (1995) Glycosylation of the variable region of immunoglobulin G-site specific maturation of the sugar chains. Mol Immunol. 32(13), 931-940. 

Adhesion proteins in this group contain an immunoglobulin domain that is composed of 90-100 amino acids arranged in a sandwich of two sheets of antiparallei strands. Some members of this family also contain fibronectin type III—like domains in addition to the immunoglobulin domain. Immunoglobulin-related adhesion proteins either can exist as transmembrane structures or can be attached to cell membranes via glycosyl phosphatidylinositol links (B4, R5). 

Type G immunoglobulins (igC) are quantitatively the most important antibodies in the blood, where they form the fraction of y-glob-ulins (see p. 276). IgGs (mass 150 kDa) are tetramers with two heavy chains (H chains red or orange) and two light chains (L chains yellow). Both H chains are glycosylated (violet see also p. 43). 

Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. 2007. The impact of glycosylation on the biological function and structure of human immunoglobulins. Ann Rev Immunol. 25 21-50. 

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