Annals of Clinical Trials and Vaccines Research

Immunoglobulin Scholarly

 In 1890, von Behring and Kitasato reported the existence of an agent within the blood that would neutralize diphtheria toxin. the subsequent year, reference was made to ‘Antikörper’, or antibodies, in studies describing the power of the agent to discriminate between two immune substances. Subsequently, the substance which induces the assembly of an antibody was mentioned because the ‘Antisomatogen+Immunkörperbildner’, or that agent which induces the antibody. The term antigen may be a contraction of this term. Thus, an antibody and its antigen represent a classic tautology.     Absorption of the serum against the antigen depleted the gamma-globulin fraction, yielding the terms human gamma globulin , immunoglobulin (Ig), and IgG. “Sizing” columns were then wont to separate immunoglobulins into people who were “heavy” (IgM), “regular” (IgA, IgE, IgD, IgG), and “light” (light chain dimers).More than 100 years of investigation into the structure and performance of immunoglobulin has only served to stress the complex nature of this protein. Typically, receptors bind to a limited and defined set of ligands. However, while individual immunoglobulin also bind a limited and defined set of ligands, immunoglobulins as a population can bind to a virtually unlimited array of antigens sharing little or no similarity. This property of adjustable binding depends on a posh array of mechanisms that alter the DNA of individual B cells. Immunoglobulins also serve two purposes: that of cell-surface receptors for antigen which enable cell signaling and cell activation which of soluble effector molecules which may individually bind and neutralize antigens at a distance.

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