Ad
related to: igg subclass 3 high
Search results
Results From The WOW.Com Content Network
The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.
IgG1 is present in the bloodstream at a percentage of about 60-70%, IgG2-20-30%, IgG3 about 5-8 %, and IgG4 1-3 %. IgG subclass deficiencies affect only IgG subclasses (usually IgG2 or IgG3), with normal total IgG and IgM immunoglobulins and other components of the immune system being at normal levels.
Despite the high sequence similarity (90% identical on the amino acid level), each subclass has a different half-life, a unique profile of antigen binding and distinct capacity for complement activation. IgG1 antibodies are the most abundant IgG class and dominate the responses to protein antigens.
The approximate length of a light chain protein is from 211 to 217 amino acids. [3] The constant region determines what class (kappa or lambda) the light chain is. [ 8 ] The lambda class has 4 subtypes ( λ {\displaystyle \lambda } 1 , λ {\displaystyle \lambda } 2 , λ {\displaystyle \lambda } 3 , and λ {\displaystyle \lambda } 7 ).
Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains.These chains are held together by disulfide bonds.The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.
Mechanism of class-switch recombination that allows isotype switching in activated B cells. Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a biological mechanism that changes a B cell's production of immunoglobulin from one type to another, such as from the isotype IgM to the isotype IgG. [1]
In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (C H domains 2–4) in each polypeptide chain.
Antibody-mediated opsonisation (marking) of pathogens depends on high affinity paratope-epitope interactions. Immunoglobulins are highly effective opsonins, with the IgG subclasses IgG1 and IgG3 being recognised as the most efficacious opsonins in humans. [1] Antibodies structurally contain two important domains