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Department of Biochemistry, Jefferson Medical College, Philadelphia, Pennsylvania
Abstract
When the products of digestion of human immunoglobulin G with pepsin are compared to those obtained with papain, one major difference appears to involve the recovery of the Fc fragment. An Fc-like fragment was isolated from peptic digests of a variety of human immunoglobulin G preparations, including 10 different samples obtained from persons with multiple myeloma. Starch gel electrophoresis showed all isolated preparations to be heterogeneous and the patterns unrelated to some known immunoglobulin subgroups and genetic factors. The preparations were Gm(a+) but Gm(y-), Gm(f-) and Gm(z-). They failed to react with rheumatoid factor and serum complement. Their structural and functional characteristics were compared to the Fc and F'c fragments obtained on digestion of immunoglobulin G with papain.
Footnotes
Supported by Grants AM 07506 and AM 11640 from the National Institute of Arthritis and Metabolic Diseases, United States Public Health Service.
2 Senior Investigator, The Arthritis Foundation.
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