immunoglobulin

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immunoglobulin:

see antibodyantibody,
protein produced by the immune system (see immunity) in response to the presence in the body of antigens: foreign proteins or polysaccharides such as bacteria, bacterial toxins, viruses, or other cells or proteins.
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; immunityimmunity,
ability of an organism to resist disease by identifying and destroying foreign substances or organisms. Although all animals have some immune capabilities, little is known about nonmammalian immunity.
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; immunologyimmunology,
branch of medicine that studies the response of organisms to foreign substances, e.g., viruses, bacteria, and bacterial toxins (see immunity). Immunologists study the tissues and organs of the immune system (bone marrow, spleen, tonsils, thymus, lymphatic system),
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Immunoglobulin

Any of the glycoproteins in the blood serum that are induced in response to invasion by foreign antigens and that protect the host by eradicating pathogens. Antibodies belong to this group of proteins. An antigen is any substance capable of inducing an immune response. Intact antigens are able to specifically interact with the induced immunoglobulins. Normally, the immune system operates in a state known as self-tolerance, and does not attack the host's own tissues, but occasionally the immune system targets host-specific antigens, resulting in autoimmune disease. See Autoimmunity

Immunoglobulins are composed of two identical heavy (H) and two identical light (L) polypeptide chains. Each H and L chain has an amino-terminal variable (V) region and a carboxyl-terminal constant (C) region. Although V regions from different antibodies exhibit considerable sequence variation, there is a large degree of sequence similarity among C regions of different antibodies. In the living animal, antibodies first bind to antigen at the antigen combining site and then, ideally, eliminate it as a threat to the host.

Immunoglobulins are heterogeneous with respect to charge, size, antigenicity, and function. There are three categories of antigenic determinants present on immunoglobulins: isotypes are found in all individuals, allotypes are found in some individuals, and idiotypes are associated with the amino-terminal variable region. Isotypic determinants are located on the carboxyl-terminal constant region and are used to group immunoglobulin H and L chains into isotypes or classes. In total, there are five human H-chain classes. IgM contains mu (μ) H chains, IgG contains gamma (γ) H chains, IgA contains alpha (α) H chains, IgD contains delta (δ) H chains, and IgE contains epsilon (ε) H chains. IgG has four subclasses, IgG1, IgG2, IgG3, and IgG4, while IgA has two subclasses, IgA1 and IgA2. There are two L-chain isotypes named kappa (κ) and lambda (λ). Kappa and lambda chains may be associated with H chains of any isotype, and a complete description of an immunoglobulin molecule requires identification of both H and L chains.

IgG is the most abundant immunoglobulin class in the serum. IgG isotypes are associated with complement fixation, opsonization (that is, rendering more susceptible to phagocytosis), fixation to macrophages, and membrane transport. Of the two IgA subclasses, IgA1 is the predominant subclass of IgA in human serum. IgA1 is the dominant subclass in all external secretions, including milk, saliva, tears, and bronchial fluids. The percentage of subclass IgA2 is higher in these fluids than in serum. IgM is the first immunoglobulin to appear during the primary immune response. IgD and IgE are present in minute amounts in normal human serum. No function has been clearly attributed to IgD. IgE is active against parasites and acts as a mediator of immediate hypersensitivity. See Anaphylaxis, Antibody, Antigen, Antigen-antibody reaction, Hypersensitivity, Immunology, Protein

McGraw-Hill Concise Encyclopedia of Bioscience. © 2002 by The McGraw-Hill Companies, Inc.

immunoglobulin

[¦im·yə·nō′glä·byə·lən]
(immunology)
Any of a set of serum glycoproteins which have the ability to bind other molecules with a high degree of specificity. Abbreviated Ig.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
Intravenous immunoglobulin for the treatment of Kawasaki disease.
Efficacy of low dose intravenous immunoglobulins in children with toxic epidermal necrolysis: an open uncontrolled study.
Lammers, "Response to intravenous immunoglobulins and placebo in a patient with narcolepsy with cataplexy," Journal of Neurology, vol.
Tavakolpour, "The role of intravenous immunoglobulin in treatment of mucous membrane pemphigoid: a review of literature," Journal of Research in Medical Sciences, vol.
Miquel et al., "Expansion of [CD4.sup.+][CD5.sup.+] regulatory T cells by intravenous immunoglobulin: a critical factor in controlling experimental autoimmune encephalomyelitis," Blood, vol.
Intravenous immunoglobulin G therapy in streptococcal toxic shock syndrome: a European randomized, double-blind, placebo-controlled trial.
The decision was made to start the patient on intravenous immunoglobulins (IVIG) while investigating for cerebrovascular accident.
Merwick et al., "Drug induced aseptic meningitis caused by intravenous immunoglobulin therapy," Irish Medical Journal, vol.
Coronary artery lesions (CALs) develop in 15–25% of untreated children with KD.[sup][6] Despite appropriate therapy with intravenous immunoglobulin (IVIG), CALs continue to develop in 5% of the affected children.
Janowicz et al., "Results of a prospective controlled two-dose crossover study with intravenous immunoglobulin and comparison (retrospective) with plasma treatment," Clinical Immunology and Immunopathology, vol.
The store's specialty pharmacy services offer medication management for people with complex diseases and chronic conditions, such as HIV, hepatitis C, dermatological conditions, intravenous immunoglobulin and rheumatoid arthritis.
After extensive discussion & review of all the available literature intravenous immunoglobulin was administered in optimal dose.

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