IgM: Difference between revisions

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IgM stands for '[[Immunogobulin M|Immunogobulin M]]'. It is an [[antibody|antibody]] that is mainly concentrated in the [[Blood|blood]] and is the first to act in the primary [[Antibody|antibody]] response to a [[Pathogen|pathogen]]/[[Antigen|antigen]]&nbsp;<ref>Molecular Biology of the Cell, fifth edition, Alberts et al, Garland Science. pages 1553-1554</ref>. IgM binds tightly to [[anitgen|anitgens]] containing multiple identical [[epitopes|epitopes]] due to the presence of 10 combining sites. In [[proteins|proteins]], avidity describes the strength of multiple bonds whereas affinity denotes the binding of a single site&nbsp;<ref>Biochemistry - Berg, Stryer and Tymoczko 2011</ref>.
IgM stands for '[[Immunogobulin M|Immunogobulin M]]'. It is an [[Antibody|antibody]] that is mainly concentrated in the [[Blood|blood]] and is the first to act in the primary [[Antibody|antibody]] response to a [[Pathogen|pathogen]]/[[Antigen|antigen]]&nbsp;<ref>Molecular Biology of the Cell, fifth edition, Alberts et al, Garland Science. pages 1553-1554</ref>. IgM binds tightly to [[Anitgen|anitgens]] containing multiple identical [[Epitopes|epitopes]] due to the presence of 10 combining sites. In [[Proteins|proteins]], avidity describes the strength of multiple bonds whereas affinity denotes the binding of a single site&nbsp;<ref>Biochemistry, Seventh Edition, Berg et al, p1022</ref>.  


=== References  ===
=== References  ===


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Revision as of 21:14, 21 October 2012

IgM stands for 'Immunogobulin M'. It is an antibody that is mainly concentrated in the blood and is the first to act in the primary antibody response to a pathogen/antigen [1]. IgM binds tightly to anitgens containing multiple identical epitopes due to the presence of 10 combining sites. In proteins, avidity describes the strength of multiple bonds whereas affinity denotes the binding of a single site [2].

References

  1. Molecular Biology of the Cell, fifth edition, Alberts et al, Garland Science. pages 1553-1554
  2. Biochemistry, Seventh Edition, Berg et al, p1022