Degradation of Immunoglobulin G by Lysosomal Acid Proteases

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...

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Veröffentlicht in:	The Journal of immunology (1950) 1970-10, Vol.105 (4), p.973-983
Hauptverfasser:	Fehr, Kurt, LoSpalluto, Joseph, Ziff, Morris
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antigens - analysis Cathepsins - pharmacology Cattle Chromatography, DEAE-Cellulose Humans Immunochemistry Immunodiffusion Immunoglobulin G Lysosomes - enzymology Molecular Weight Peptide Hydrolases - pharmacology Spleen - enzymology Synovial Membrane - enzymology Ultracentrifugation
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