A STUDY OF THE COMPETITION OF LECITHIN AND ANTITOXIN FOR CL. WELCHII LECITHINASE.
Lecithin has been found to interfere with the combining reaction of Cl. welchii alpha toxin (lecithinase) and its antitoxin. If the lecithinase is first brought into contact with lecithin, and the antitoxin is then added, the antitoxin fails to stop the enzymatic reaction, but gradually decelerates it. If the lecithinase is brought into contact with both lecithin and antitoxin at the same instant, it appears to combine in part with each, and the enzymatic process takes place at a reduced rate, which gradually declines further. If the lecithinase is first brought into contact with antitoxin, before the lecithin is added, the enzymatic reaction is completely inhibited. This ability of lecithin to inhibit the antitoxin-toxin combination cannot be explained adequately as a non-specific coating of the toxin-enzyme by the lecithin. It is rather suggested that lecithin and antitoxin compete specifically for combination with the same regions on the enzyme molecule. Lecithin has similarly been found to interfere with the combination of Crotalus terrificus venom and its antiserum. The above findings provide a partial explanation for the lack of effectiveness of antitoxin when given late in the course of Cl. welchii infection.
Zamecnik
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PC
Medical Laboratories of the Collis P. Huntington Memorial Hospital of Harvard University, and the Biochemical Research Laboratory, Massachusetts General Hospital, Boston.
Lipmann
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F
D000992:Antitoxins; D001419:Bacteria; D005734:Gangrene; D005738:Gas Gangrene; D007106:Immune Sera; D054709:Lecithins; D010713:Phosphatidylcholines; D010740:Phospholipases
D000992:Antitoxins; D007106:Immune Sera; D054709:Lecithins; D010713:Phosphatidylcholines; D010740:Phospholipases