Light polypeptide chain

The antibodies are similar in structure to other globulin proteins which are present in serum of vertebrates [9], The antibody molecule consists of two light polypeptide chains and two heavy polypeptide chains [10]. The amino acids are present in all the chains but the number of residues and the sequence will vary in different antibody multiforms [9], Light chains contain approximately 220 amino add residues and heavy chains about 450 residues. The complete sequence of the chains of human IgG myeloma protein has been determined by Edelman [11], The chains are held together in the unique conformational structure of the antibody molecule by a few covalent disulfide bonds between the chains and many electrostatic bonds between the amino groups of one chain and the hydroxyl groups of another chain. The covalent bonds are represented in Formula 1, 2 and 3 [peptide, disulfide and... 

All immunoglobulins have a number of structural features in common.2 They possess two light polypeptide chains, each with an approximate molecular weight of 25 kDa, and two heavy polypeptide chains of 50 kDa each. These four chains are bound together in a single antibody molecule by disulfide bonds, and form a Y-shape with a central axis of symmetry (Fig. 5.2). The two halves of a natural immunoglobulin are identical. 

The N-terminal ends of the light polypeptide chains (L) occur near the top of the Y structure, in the so-called Fab fragments. These are the antigen-binding... 

An IgG molecule consists of two heavy chains and two light polypeptide chains connected through disulfide bonds (Figure 1). IgG antibodies have a molecular weight of 150 Kd and account for approximately 80 ( of the total immunoglobulin in human serum. 

In this section, the determination of glyco moieties of a special class of glycoproteins, the class G immunoglobulins (IgG), is described. Immunoglobulins G consist of two heavy and two light polypeptide chains and carry their carbohydrates mainly in the conservative region of the heavy chains (Fc). Additionally,... 

The first attempt to suppress the synthesis of Ig allotypes in mice was unsuccessful. The majority of progeny from immunized mice mothers died, and surviving offspring demonstrated a normal concentration of the paternal allotype. However, Herzenberg successfully suppressed Ig synthesis with Ig-lb specificity, initially for short periods of time and then for the entire life of the mouse (Herzenberg, 1970). Recently, short-term suppression of Ig synthesis in mice was induced with the aid of antibodies to some of the determinants of the variable part of light polypeptide chains (Ruffmi et al., 1970). 

---