Протеолитическая активность дифтерийного токсина

Abstract

Purified samples of diphtheria toxin spitted human fibrinogen, human serum albumin and gelatin. Splitting was completely inhibited by nitrotetrazolium blue (0.01 mol) but no other active oxygen species. The proteolytic activity of the toxin was weakly changed in the presence of the group of specific proteinase inhibitors (0.001 mol). The comparison of inhibitor effects on the proteolytic activity of diphtheria toxin and activity of intracellular and extracellular proteinases of PW-8 proved that proteolytic activity of the toxin was not determined by the presence of residual activity of microbial proteinases. Field o f application: physiology and biochemistry of pathogenic microorganisms, enzymology, experimental medicine, medicine biotechnology. Proposals for co-operation: joint study of the problem.