Abstract
Determination of the primary structure of immunoglobulin proteins provides information that can be used to extend our knowledge of the structural relationship between different classes of immunoglobulins, as well as their genetic and evolutionary characteristics. Primary structural information will also be important ultimately in attaining an understanding of the antibody and non-antibody functional properties of these molecules.
Immunoglobulin E (IgE) is the most recently discovered of the human immunoglobulins and is the one, therefore, about which we have the least structural information. IgE antibodies bind antigens, and also have the capacity to sensitize receptors in human tissue for immediate hypersensitivity reactions (reviewed in 1). Structural studies of IgE will provide data for comparison with the amino acid sequences already determined for other classes of human immunoglobulins, and also may be useful in investigating the nature of the interaction between IgE molecules and cellular receptors.
Footnotes
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↵1 This work was aided by Grants CA 04326, Dartmouth, AM 12912, and CA 04457 (Mount Sinai) from the United States Public Health Service, and by the Albert A. List, Frederick Machlin and Anna Ruth Lowenberg Research Funds (Mount Sinai).
- Copyright, 1970, by The Williams & Wilkins Company
- Copyright © 1970 by The American Association of Immunologists, Inc.
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