Trypsin-like proteinase and its endogenous inhibitor from Yersinia pseudotuberculosis. Biological activity.
A trypsin-like proteinase (YPTP) and its endogenous inhibitor (ITYP) were isolated from the culture filtrate of the pathogenic bacterium Yersinia pseudotuberculosis, and their biological activities were studied. YPTP was found to be highly toxic for random-bred white mice. Under in vitro conditions the proteolytic enzyme destroyed protective proteins of the immune system of the animals--IgG, IgA, and proteins of the complement system (CIq, C3, and C5)--and, consequently, was a pathogenetic factor in yersinioses. The inhibitor ITYP was shown to manifest antibacterial activity against virulent forms of Yersinia pseudotuberculosis, Escherichia coli, and Salmonella typhimurium. The ITYP preparation was harmless and nontoxic.
Burtseva
T I
TI
Pacific Institute of Bioorganic Chemistry, Far Eastern Branch of the Russian Academy of Sciences, Vladivostok, 690022, Russia. elyakov@piboc.marine.su
Loenko
Y N
YN
D000818:Animals; D003165:Complement System Proteins / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D051379:Mice; D008826:Microbial Sensitivity Tests; D012486:Salmonella typhimurium / Q000187:drug effects; D014357:Trypsin / Q000302:isolation & purification / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D015011:Yersinia pseudotuberculosis / Q000187:drug effects / Q000378:metabolism* / Q000472:pathogenicity; D015012:Yersinia pseudotuberculosis Infections / Q000276:immunology*
D007074:Immunoglobulin G; D014361:Trypsin Inhibitors; D003165:Complement System Proteins; D014357:Trypsin