title: Release of thioltransferase from rabbit polymorphonuclear leucocytes by immune complex in vitro and inhibition of the enzyme by chloramphenicol.
abstract: 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).
mesh_terms: D000818:Animals; D000936:Antigen-Antibody Complex / Q000502:physiology*; D002701:Chloramphenicol / Q000494:pharmacology*; D054477:Glutaredoxins; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007526:Isoelectric Point; D009504:Neutrophils / Q000201:enzymology* / Q000276:immunology; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000097:blood*; D011490:Protein Disulfide Reductase (Glutathione); D011817:Rabbits; D015054:Zymosan / Q000494:pharmacology
chemical_list: D000936:Antigen-Antibody Complex; D054477:Glutaredoxins; D002701:Chloramphenicol; D015054:Zymosan; D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione)