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Raif S. Geha, MD

Am J Dis Child. 1985;139(4):417-420.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

Antibodies have a perfect fit with their corresponding antigens and are able to perform certain functions as a result of this binding. The antigen specificity of the antibody is determined by the variable (V) sequences of the 100 or so amino acid residues at the amino-terminal end of each of the heavy (H) and light (L) polypeptide chains of the antibody molecule (Fig 1); the remaining constant amino acid sequences from the constant (C) domains determine the class of antibodies to which the molecule belongs. Heterogeneity in the C domain distinguishes about 20 classes of immunoglobulin molecules, ie, isotypes, and distinguishes within each isotype a limited number of differences, ie, allotypes, which result from genetic polymorphism within the species. Heterogeneity in the V domain distinguishes millions of antibody molecules and forms the basis of antibody diversity.

Antibodies, being proteins, can act as antigens in the same host, resulting in the . . . [Full Text PDF of this Article]

Author Affiliations
From the Division of Allergy, Children's Hospital Medical Center, Boston.

Footnotes
Reprint requests to Division of Allergy, Children's Hospital Medical Center, 300 Longwood Ave, Boston, MA 02115 (Dr Geha).

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