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Degradation of Immunoglobulin G by Lysosomal Acid Proteases¹

From the Department of Internal Medicine (Rheumatic Diseases Unit) and the Department of Biochemistry, University of Texas Southwestern Medical School at Dallas

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

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.

² Present address: Universitäts rheumaklinik, Gloriastrasse 25, 8006 Zurich, Switzerland.

³ All correspondence should be addressed to Dr. LoSpalluto, Dept. of Biochemistry.

⁴ Recipient, Research Career Award, National Institutes of Arthritis and Metabolic Diseases, National Institutes of Health.