Abstract
Enzyme preparations from bovine spleen, human spleen, and lysosomal fractions of human synovial membrane tissue have been shown to degrade human IgG at pH 3.5. The major proteolytic activity is due to cathepsin D. The products of digestion have been shown to consist of fragments of IgG ranging from a slightly altered IgG with a molecular weight of approximately 135,000 to extensively degraded Fc and partially degraded Fab fragments.
Footnotes
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↵3 All correspondence should be addressed to Dr. LoSpalluto, Dept. of Biochemistry.
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↵4 Recipient, Research Career Award, National Institutes of Arthritis and Metabolic Diseases, National Institutes of Health.
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↵1 Supported by Grant I155, Robert A. Welch Foundation; Grant AI-05479, National Institute of Arthritis and Metabolic Diseases; and Project Grant AM-09989 from the United States Public Health Service.
- Received March 2, 1970.
- Copyright © 1970 by The American Association of Immunologists, Inc.
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