Release of thioltransferase from rabbit polymorphonuclear leucocytes by immune complex in vitro and inhibition of the enzyme by chloramphenicol.
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).
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
D000936:Antigen-Antibody Complex; D054477:Glutaredoxins; D002701:Chloramphenicol; D015054:Zymosan; D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione)