The bacteriolytic activity of interleukin-2 and chicken egg lysozyme in the
presence of various substances has been studied. Glycine and lysine do not
affect the activity of interleukin-2 but increase that of lysozyme, showing a
bell-shape concentration dependence peaking at 1.5 mM glycine and 18 mM lysine.
Arginine and glutamate activate both interleukin-2 and lysozyme with a
concentration dependence of the saturation type. Aromatic amino acids have
almost no effect on the activity of both interleukin-2 and lysozyme. Aromatic
amines, tryptamine, and tyramine activate interleukin-2 but inhibit lysozyme.
Peptide antibiotics affect interleukin and lysozyme similarly and exhibit
maximum activity in the micromolar range of antibiotics. Taurine has no effect
on the activity of interleukin-2 and lysozyme. Mildronate showed no influence
on lysozyme, but it activated interleukin-2 with the activity maximum at 3 mM.
EDTA activates both interleukin-2 and lysozyme at concentrations above 0.15 mM.