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Immune complex induced the release of thioltransferase from rabbit peritoneal exudates polymorphonuclear leucocytes in vitro. The release of thioltransferase occurs from viable cells and does not depend on a cytolysis. The catalytic activity of the released enzyme with S-sulfocysteine and glutathione as substrates had a distinct optimum pH at 7.6. On the contrary, opsonized zymosan was not effective as a stimulus for the liberation of thioltransferase from polymorphonuclear leucocytes. Thioltransferase liberated by the stimulation with immune complex was inhibited by chloramphenicol, but not by bacitracin. The inhibition was non-competitive (apparent Ki of 0.2 mM).
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