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The Journal of Immunology, 1969, 102: 1523-1525.
Copyright © 1969 by The American Association of Immunologists, Inc.

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Communications

Unusual Conditions for Crystallization of the Fc Fragment of Chicken IgG1

Ralph T. Kubo2 and Albert A. Benedict

From the Department of Microbiology, University of Hawaii, Honolulu, Hawaii 96822

Abstract

Enzymatic digestion of IgG immunoglobulins has been used extensively to study the relationship between function and structure of these proteins. Papain hydrolysis of rabbit IgG yields two kinds of fragments (1): Fab, which is composed of H- and L-chain determinants and is the structural site for antibody activity; and Fc, which contains only H-chain determinants and is crystallizable. The Fc fragment has been crystallized from rabbit IgG (1), human IgG (2), and guinea pig IgG (3). The conditions for formation of Fc crystals generally require dialysis against distilled water or low ionic strength buffers in the cold. Chicken IgG also is hydrolyzed by papain into Fab and Fc fragments (4–7), but crystalline like structures rarely have been seen in the Fc preparations. Evidence is given here that chicken Fc is easily crystallized under conditions quite unlike those used for the crystallization of Fc from mammalian IgG.

Footnotes

This investigation was supported by United States Public Health Service Training Grant AI-00243-06 from the National Institute of Allergy and Infectious Diseases.

2 Predoctoral Trainee.







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