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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.
- Structure and Function of Immunoglobulins
Immunoglobulins are heterodimeric proteins composed of two...
- Structure and Function of Immunoglobulins
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.
Affinity of the antibody for the epitope (see above) Valency of both the antibody and antigen Structural arrangement of the parts that interact All antibodies are multivalent e.g. IgGs are bivalent and and IgMs are decavalent. The greater an immunoglobulin’s valency (number of antigen binding sites), the greater the amount of antigen it can bind.
Antibody affinity is defined as strength of the binding interaction between antigen and antibody. It depends on the closeness of the stereochemical fit between antibody sites and antigen determinants, the size of the area of contact between them, and the distribution of charged and hydrophobic groups.
Affinity maturation is the process by which antibodies gain increased affinity, avidity, and anti-pathogen activity and is the result of somatic hypermutation (SHM) of immunoglobulin genes in B cells, coupled to selection for antigen binding ( Figure 1 ).
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.
