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  1. 16 de abr. de 2009 · Abstract. Distinct genes encode 6 human receptors for IgG (hFcγRs), 3 of which have 2 or 3 polymorphic variants. The specificity and affinity of individual hFcγRs for the 4 human IgG subclasses is unknown. This information is critical for antibody-based immunotherapy which has been increasingly used in the clinics.

  2. 8 de sept. de 2020 · Immunoglobulin E. IgE is a monomer. It has a molecular weight of 188 Kd and a serum concentration of 0.00005 mg/mL. It protects against parasites and binds to high-affinity receptors on mast cells and basophils, causing allergic reactions.

  3. The FcγR differ in their binding affinity to IgG, with FcγRI showing the highest affinity whereas FcγRII and FcγRIII bind with lower affinity. For that reason, only FcγRI binds monomeric IgG while the other two receptors bind aggregated IgG or immune complexes.

  4. Affinity measures the strength of interaction between an epitope and an antibody’s antigen binding site. It is defined by the same basic thermodynamic principles that govern any reversible biomolecular interaction:

  5. 17 de abr. de 2020 · Affinity and avidity are two terms used in immunology and microbiology to describe binding strength between an antibody and antigen. Because both affinity and avidity involve binding strength, the two terms are often confused.

  6. 30 de abr. de 2015 · Human Fcγ receptor I (hFcγRI) binds IgGs with high affinity and is the only Fcγ receptor that can effectively capture monomeric IgGs. However, the molecular basis of hFcγRI’s interaction...

  7. The antibodies produced initially in response to most antigens are high molecular weight (MW) immunoglobulins (IgM) with low affinity for the antigen, while the antibodies produced later are lower MW classes (e.g., IgG and IgA) with, on average, orders of magnitude higher affinity for that antigen.