Immunoglobulin: Difference between revisions
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Immunogolbulin molecules have different heavy chains depending on the class (IgM, A, D, G, E), | |||
IgM - μ chains | |||
IgA - α chains | |||
IgD - δ chains | |||
IgG - γ chains | |||
IgE - ε chains | |||
<references /><ref>Berg, JM. Tymoczko, JL. Stryer, L. (2012) Biochemistry (7), p. 1022-1023.</ref> | |||
Revision as of 23:22, 19 October 2017
Immunoglobulins are antibody molecules. They are proteins used in the immune response to identify and attach to antigens. There are five classes of immunoglobulin - IgA, IgD, IgE, IgG and IgM. All of the classes have two identical heavy chains which are bound to two identical light chains. The classes are distinguished by their structure and function, where for example, IgM is a pentamer and IgA is a dimer[1]. Each class plays a different role in adapive immune response.
Reference
- ↑ Lodish, HF (2013). Molecular cell biology. 7th ed. New York: W.H. Freeman . 1068-1069.
Immunogolbulin molecules have different heavy chains depending on the class (IgM, A, D, G, E),
IgM - μ chains
IgA - α chains
IgD - δ chains
IgG - γ chains
IgE - ε chains
- ↑ Berg, JM. Tymoczko, JL. Stryer, L. (2012) Biochemistry (7), p. 1022-1023.