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Biochemistry (Moscow)

, Volume 79, Issue 1, pp 1–7 | Cite as

The second life of antibodies

  • E. V. NavolotskayaEmail author
Review

Abstract

Antibodies (immunoglobulins, Ig) are used by the immune system to identify and neutralize foreign objects and are responsible for antigen-binding and effector functions. Immunoglobulin G (IgG) is the major serum immunoglobulin of a healthy human (∼75% of the total Ig fraction). The discovery in 1970 of the endogenous tetrapeptide tuftsin (Thr-Lys-Pro-Arg, fragment 289–292 of the CH2-domain of the heavy (H) chain of IgG), possessing both immunostimulatory and neurotrophic activities, was an impetus for the search for new biologically active peptides of immunoglobulin origin. As a result, fragments of the H-chain of IgG produced as a result of enzymatic cleavage of IgG within the antigen-antibody complex were discovered, synthesized, and studied. These fragments include rigin (341–344), immunorphin (364–373), immunocortin (11–20), and peptide p24 (335–358) and its fragments. In this review the properties of these peptides and their role in regulating the immune response are analyzed.

Key words

antibodies peptides receptors immune system 

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© Pleiades Publishing, Ltd. 2014

Authors and Affiliations

  1. 1.Branch of Shemyakin-Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesPushchino, Moscow RegionRussia

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