Characterization of anti-treponemal lymphotoxin from lymphocytes of syphilitic rabbits.
The effect of various treatments on the activity of anti-treponemal lymphotoxin (ATL) produced by lymphocytes of syphilitic rabbits was studied. Treponema pallidum-killing activity of ATL was slightly reduced after heating at 56 degrees C and completely abolished at 100 degrees C. The significant reduction of the activity was also obtained after exposure of ATL to acidic conditions (pH 1-5) at room temperature, or by treatment with papain and neuraminidase. Activity of ATL was completely resistant to deoxyribonuclease, ribonuclease and trypsin treatment. ATL was eluted from the Sephadex G-100 column together with hemoglobin, that suggested the apparent molecular weight of ATL of about 65,000. The active fraction from the Sephadex G-100 column was further fractionated on DEAE-Sephadex A-50. The activity of ATL was widely spread in the column eluate, indicating the charge heterogeneity. All these data indicate that ATL is a relatively low molecular weight protein. The sensitivity to neuraminidase and heterogeneity of charge suggest that it is a glycosylated protein.
D000818:Animals; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008214:Lymphocytes / Q000276:immunology*; D008233:Lymphotoxin-alpha / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D008970:Molecular Weight; D009005:Monosaccharides / Q000494:pharmacology; D009439:Neuraminidase / Q000494:pharmacology; D011817:Rabbits; D013587:Syphilis / Q000276:immunology*; D014210:Treponema pallidum / Q000276:immunology*
D008233:Lymphotoxin-alpha; D009005:Monosaccharides; C042270:anti-treponemal lymphotoxin; D009439:Neuraminidase