RESUMEN
New glycolipids, derived from chitooligosaccharides of dp 2-4 and containing both free and acylated amino groups, were synthesized. The structure of the key compounds (di-, tri-, and tetra-saccharides acylated with different fatty acids) were elucidated by 13C NMR spectroscopy. Only the amino group of the reducing end of the chitooligosaccharides was found to be acylated when equimolecular amounts of reagents were used. The compounds obtained were shown to possess a low toxicity and certain immunostimulatory and antitumor activities. An induction of interleukin-1 and tumor necrosis factor by the immunocompetent cells and an augmentation by 140-180% of the mean life of mice with the Erlich carcinoma were observed.
Asunto(s)
Adyuvantes Inmunológicos/farmacología , Antineoplásicos/farmacología , Quitina/farmacología , Glucolípidos/farmacología , Oligosacáridos/farmacología , Adyuvantes Inmunológicos/química , Animales , Antineoplásicos/química , Antineoplásicos/inmunología , Secuencia de Carbohidratos , Quitina/química , Glucolípidos/química , Glucolípidos/inmunología , Masculino , Ratones , Ratones Endogámicos CBA , Datos de Secuencia Molecular , Oligosacáridos/químicaRESUMEN
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.