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Immunoglobulins are heterodimeric proteins composed of two heavy (H) and two light (L) chains. They can be separated functionally into variable (V) domains that binds antigens and constant (C) domains that specify effector functions such as activation of complement or binding to Fc receptors.
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.
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.
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.
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 with Fc...
The family of Fc receptors for IgG (FcγRs) is broadly expressed by cells of haematopoietic origin and consists of one inhibitory and several activating receptors that differ in their affinity and...
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.
