Abstract
Summary
Reduced crystalline papain inactivated the pyrogenic and lethal activities of purified Gram-negative bacterial endotoxins. Because of the possible presence of peptide, ester and amide linkages within the macromolecular toxin and the known ability of the enzyme to split linkages of all 3 types, it was not possible from these results to implicate a specific linkage or group in endotoxin activity. It was suggested that this purified enzyme may prove useful for further studies on the chemical nature of the active groups within the endotoxin molecule.
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