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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.
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.
Antibody Affinity. 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: KA = affinity constant. [Ab] = molar concentration of unoccupied binding sites on the antibody.
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.
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...
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.
