Degradation of Immunoglobulins by Intracellular Proteases in the Range of Neutral pH

A proteolytic enzyme active in the range of neutral or slightly alkaline pH has been partially purified from a lysosome-containing granule fraction of human spleen. The molecular weight of the enzyme was estimated to be in the range of 15,000 to 30,000 by gel filtration, and it has a pH optimum of a...

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Veröffentlicht in:	The Journal of immunology (1950) 1970-10, Vol.105 (4), p.886-897
Hauptverfasser:	LoSpalluto, Joseph J, Fehr, Kurt, Ziff, Morris
Format:	Artikel
Sprache:	eng
Schlagworte:	Albumins Animals Chromatography Chromatography, Gel Cysteine - pharmacology Electrophoresis Enzyme Activation Epitopes - analysis Gels Goats Hemoglobins Humans Hydrogen-Ion Concentration Immunochemistry Immunodiffusion Immunoglobulin G Immunoglobulin M Immunoglobulins Isoflurophate - pharmacology Lysosomes - enzymology Molecular Weight Papain - pharmacology Peptide Hydrolases Spleen - enzymology Ultracentrifugation
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