The antigen-binding site is the area of the antibody that recognizes and binds to the antigen. Photo Credit: Image Credit: Darryl Leja, NHGRI. Antibodies (also called immunoglobulins) are specialized proteins that travel thorough the blood stream and are found in bodily fluids.
http://biology.about.com/od/molecularbiology/ss/antibodies.htm
The term immunoglobu-lin can be used to refer to any antibody-like molecule,regardless of its antigen-binding specificity. 3 THE STRUCTURE OF AN ANTIBODY IS RELATEDTO ITS FUNCTION The function of an antibody is to bind foreign or non-self molecules.
http://www.wiley.com/legacy/products/subject/life/elgert/CH04.pdf
The large and diverse population of antibody paratope is generated by random recombination events of a set of gene segments that encode different antigen-binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity.
https://en.wikipedia.org/wiki/Antibody
At the ends of both the heavy and light chains, in the areas that form the arms of the Y-shaped structure, are regions known as antigen-binding sites. The antigen-binding site is the area of the antibody that recognizes the specific antigenic determinant and binds to the antigen. Since different antibodies recognize different antigens, antigen-binding sites are different for different antibodies. This area of the molecule is known as the variable region.
http://biology.about.com/od/molecularbiology/ss/antibodies.htm
Antibodies recognize specific antigens by identifying certain areas on the surface of the antigen known as antigenic determinants. Once the specific antigenic determinant is recognized, the antibody will bind to the determinant. The antigen is tagged as an intruder and labeled for destruction by other immune cells.
http://biology.about.com/od/molecularbiology/ss/antibodies.htm
This region is known as the hypervariable region. Each of these variants can bind to a different antigen. This enormous diversity of antibody paratopes on the antigen-binding fragments allows the immune system to recognize an equally wide variety of antigens.
https://en.wikipedia.org/wiki/Antibody
Though strictly speaking, an antibody is not the same as an immunoglobulin; B cells can produce two types of immunoglobulins-surface immunoglobulins, which are B cell receptors; and secreted immunoglobulins, which are antibodies. So antibodies are one of two classes of immunoglobulins.
https://en.wikipedia.org/wiki/Antibody
The antigen-binding sites of an antibody molecule are located inthe (a) C region of light chains, (b) V region of light chains, (c)C region of heavy chains, (d) V region of heavy chains, (e) re-gions of both light and heavy chains, (f) none of these. (Seepages 63, 64, and 67) 4.
http://www.wiley.com/legacy/products/subject/life/elgert/CH04.pdf
IgM isthe first antibody to appear during an immune re-sponse and the first formed by a developing fetus. Be-cause of its many antigen-binding sites, IgM canquickly clump antigen and efficiently activate comple-ment. IgM acts as one of the main receptors on the sur-face of mature B cells, along with IgD.
http://www.wiley.com/legacy/products/subject/life/elgert/CH04.pdf
Each antibody binds to a specific antigen; an interaction similar to a lock and key. An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shape protein produced by plasma cells that is used by the immune system to identify and neutralize pathogens such as bacteria and viruses. The antibody recognizes a unique molecule of the harmful agent, called an antigen, via the variable region.
https://en.wikipedia.org/wiki/Antibody
what are the antigen binding sites of immunoglobulins made of
The antigen binding sites of immunoglobulins are made of the plasma cells. The antigen binding sites of immunoglobulins are made of Plasma cells. 