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Immunoglobulin G (IgG1) molecule images
Immounoglobulins (antibodies) are the glycoproteins involved in immune response. They possess ability to recognize antigens and bind them. Immunoglobulins could be found as in plasma, as linked to lymphocytes cellular membrane. The molecule is comprised of two identical s.c. light chains and two heavy chains, linked by disulphide bridges [1]. The characteristic feature of the antibodies is the highly variable sequence pattern, recognizing and specifically binding to the exposed antigen. Due to this feature immune system could react to the broad range of allogenic agents. Variable regions are located at Immunoglobulins are separated in 5 subclasses: IgG, IgA, IgM, IgD and IgE. The classes distinguish by localization, prevalence, role and participation timing in immune response. In addition, they are different by the structure and shape, especially in non-variable part [3]. The model presented provides the view of the common IgG1 protein. Light chains are shown in red, heavy are in grey, disulphides linking chains one to other are in yellow, oligosaccharide is in dark grey. |
Cast:
1. Meulenbroek A.J., Zeijlemaker W.P. Human IgG Subclasses: Useful diagnostic markers for immunocompetence. Published by Sanquin formerly CLB (Centraal Laboratorium van de Bloedtransfusiedienst) Plesmanlaan 125, 1066 CX Amsterdam, The Netherlands. CLB (1996) 2. Stitis, D.P., J.D. Stobo, J.V. Wells: «Basic and Clinical Immunology» 7th edition, Appleton and Lange (1991) 3. Koolman J., Rohm 4. Spiegelberg H.L.: «Biological activities of Igs of different classes and subclasses». Adv.Immunol.19, 259 (1974) 5. Burton, D.R., L. Gregory and L. Jefferis:«Aspects of the Molecular Structure of the IgG subclasses». Monograph. Allergy 19,7 (1986) |
