| Autor: |
David O. Beenhouwer, S. L. Morrison, K. R. Chintalacharuvu |
| Rok vydání: |
2003 |
| Předmět: |
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| Zdroj: |
Monoclonal Gammopathies and the Kidney ISBN: 9789048161997 |
| DOI: |
10.1007/978-94-017-0191-4_2 |
| Popis: |
Immunoglobulins (antibodies) are a family of glycoproteins that are produced by plasma cells. All immunoglobulin molecules consist of a unit composed of two identical light (L) chain polypeptide chains and two identical heavy (H) polypeptide chains linked together by disulfide bonds (H2L2). The L and H chains fold into functional domains, two for the L chain and four or five for the H chain. The N-terminal domain from each chain forms the variable regions, VL and VH, which together constitute the antigen-binding site. The rest of the molecule has a relatively constant (C) structure. The variable regions with the constant region of the L chain and the first constant region domain of the H chain constitute an Fab region. The remaining constant region domains of the H chain make up the Fc region. Immunoglobulin molecules follow several different assembly and secretion pathways and have characteristic post-translational modifications that can contribute to their diverse functional capacities. Alterations in post-translational modification can be associated with significant diseases such as rheumatoid arthritis1,2 and IgA nephropathy3,4. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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