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    Academic Journal

    Contributors: РФФИ, гранты 07-04-00100а, 08-0400731а.

    Source: Problems of Particularly Dangerous Infections; № 2(96); 29-32 ; Проблемы особо опасных инфекций; № 2(96); 29-32 ; 2658-719X ; 0370-1069 ; 10.21055/0370-1069-2008-2(96)

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    Relation: https://journal.microbe.ru/jour/article/view/1054/960; Джапаридзе М.Н. Каталазная и пероксидазная активность чумного и псевдотуберкулезного микробов [дис. канд. мед. наук]. 1953. 205 с.; Куликов О.А., Дробков В.И., Дармов И.В. и др. Супероксиддисмутазы чумного микроба. Вестн. Рос. АМН. 1996; 6:45-9.; Куклева Л.М., Проценко О.А., Кутырев В.В. Современные представления о родстве возбудителей чумы и псевдотуберкулеза. Мол. генет., микробиол. и вирусол. 2002,1:3-7.; Шиманюк Н.Я., Асеева А.Е., Мишанькин Б.Н. Супероксиддисмутазная активность у иерсиний. В кн.: Иерсиниозы: микробиол., эпидемиол., клиника, патогенез, иммунол. Владивосток; 1968. С. 83-84.; Babior B. Oxygen-dependent microbial killing by phagocytes. New Engl. J. Med: 1978; 289: 659-68.; Beaman B., Black C., Doughty F., et al. Role of superoxide dismutase and catalase as determinants of pathogenicity of Nocardia asteroids: importance in resistance to microbicidal activities of human polymorphonuclear neutrophils. Infect. Immun. 1985; 47: 135-41.; Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 1971; 44: 276-87.; Beyer W., Fridovich I. Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions. Anal. Biochem. 1987; 161: 559-66.; Brot N., Weissbach L., Werth J., et al. Enzymatic reduction of protein-bound methionine sulfoxide. Prot. Natl. Acad. Sci USA. 1981; 78:2155-58.; Burrows T., Farrel J., Gillett W. The catalase activity of Pasteurella pestis and other bacteria. Br. J. Exp. Pathol. 1964; 45:579-88.; Cohen H. The use of diaminobenzidine for spectrophotometric and acrylamide gel detection of sulfite oxidase and its applicability to hydrogen peroxide-genereting enzymes. Anal. Biochem. 1973; 53:208-22.; Davis B. Disc electrophoresis. II. Method and application to human serum proteins. Ann. N.Y. Acad. Sci. 1964; 121:404-27.; Fridovich I. Oxygen radicals, hydrogen, peroxide and oxygen toxicity. In: W.A. Prior, editor. Free radicals in biology. New York: Academic Press; 1976. p. 239-277.; Fridovich I. The biology of oxygen radicals. Science. 1978; 201:875-80.; Carcia E., Nedialkov Y., Elliott J., et al. Molecular characterization of KatY (Antigen 5), a thermoregulated chromosomally encoded catalase-peroxidase of Yersinia pestis. J. Bacteriol. 1999; 181(10):3114-22.; Gregory E., Fridovich I. Visualization of catalase in acrylamide gels. Analyt. Biochem. 1974; 58:57-62.; Hollsstein M., Brooks P., Linn S., et al. Hydroxymethyluracil DNA glycosylase in mammalian cells. Proc. Natl. Acad. Sci. USA. 1984; 81:4003-7.; Mandell G. Catalase, superoxide dismutase and virulence in Staphylosossus aureus: in vitro and in vivo studies with emphasis on staphylococcal-leukocyte intraction. J. Clin. Invest. 1975; 55: 561-66.; Marcheva D., Nicolova S., Veljanov D. О распространении каталазной активности у бактерий рода Yersinia. Докл. Болг. АН. 1988; 41(3):57-60.; Mead J. Free radical mechanism of lipid damage and consequences for cellular mambranes. In: W.A. Prior, editor. Free radicals in biology. New York: Academic Press; 1976. P. 51-68.; Mehigh R., Brubaker R. Major stable peptides of Yersinia pestis synthesized during the low-calcium response. Infect. Immun. 1993; 61(1):13-22.; Raymond S. Acrylamide gel electrophoresis. Ann. N.Y. Acad. Sci. 1964; 121:350-65.; Rockenmacher M. Relationship of catalase activity to virulencein Pasteurella pestis. Proc. Soc. Exp. Biol. Med. 1949; 71:99-101.; Selander R., Caugant D., Ochman H., et al. Methods of multilocus enzyme electrophoresis for bacterial population genetics and systematics. Appl. Environ. Microbiol. 1986; 51:873-84.; Vassilyadi M., Archibald F. Catalase, superoxide dismutase and production of O2-sensitive mutants of Bacillus coagulans. Can. J. Microbiol. 1985; 31:994-99.; https://journal.microbe.ru/jour/article/view/1054

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