Presence of the arginine dihydrolase pathway in Mycoplasma.
نویسندگان
چکیده
Barile, Michael F. (Division of Biologics Standards, National Institutes of Health, Bethesda, Md.), Robert T. Schimke, and Donald B. Riggs. Presence of the arginine dihydrolase pathway in Mycoplasma. J. Bacteriol. 91:189-192. 1966.-The presence of the arginine dihydrolase pathway was examined in 61 Mycoplasma strains representing at least 18 Mycoplasma species isolated from nine different sources: human, bovine, avian, murine, swine, goat, canine, sewage, and tissue cell culture origin. Some species were represented by only one or two strains. Different strains of the same species gave the same results. Ten species (56%) were positive. Many nonpathogenic Mycoplasma species (M. hominis, type 1 and 2, M. fermentans, M. salivarium, and M. gallinarum) were positive, whereas most pathogenic species (M. pneumoniae, M. gallisepticum, M. neurolyticum, and M. hyorhinis) were negative. The presence of arginine dihydrolase activity among Mycoplasma species may prove to be useful for purposes of identification and classification.
منابع مشابه
Arginine Metabolism in Pleuropneumonia-like Organisms Isolated from Mammalian Cell Culture.
Schimke, Robert T. (National Institutes of Health, Bethesda, Md.) and Michael F. Barile. Arginine metabolism in pleuropneumonia-like organisms isolated from mammalian cell culture. J. Bacteriol. 86:195-206. 1963.-Arginine degradation is a significant metabolic process for pleuropneumonia-like organisms (PPLO; Mycoplasma) isolated from cell culture. The conversion of arginine to ornithine in PPL...
متن کاملArginine metabolism in Trichomonas vaginalis infected with Mycoplasma hominis
Both Mycoplasma hominis and Trichomonas vaginalis utilize arginine as an energy source via the arginine dihydrolase (ADH) pathway. It has been previously demonstrated that M. hominis forms a stable intracellular relationship with T. vaginalis; hence, in this study we examined the interaction of two localized ADH pathways by comparing T. vaginalis strain SS22 with the laboratory-generated T. vag...
متن کاملArginine catabolism by Mycoplasma meleagridis and its role in pathogenesis.
A thin-layer chromatography technique was used to study the arginine metabolism of Mycoplasma meleagridis. The technique reflected the enzyme activity of the dihydrolase pathway through detection of readily visible end products on X-ray film. Strains of M. meleagridis differing in their pathogenicity for turkeys did not vary in arginine metabolism. In addition, no significant difference was obs...
متن کاملThe formation of arginine dihydrolase by streptococci and some properties of the enzyme system.
The lack of any breakdown of urea under the experimental conditions led to the conclusion that urease was not present in streptococci and that urea could not be an intermediate in the reaction. Thus it seems likely that the formation of ornithine from arginine by these bacteria occurred by a pathway different from that possessed by arginase of mammalian liver. Niven et al. (1942) tested the abi...
متن کاملRegulation of the arginine dihydrolase pathway in Clostridium sporogenes.
Arginine deiminase activity was induced during the vegetative growth of Clostridium sporogenes. The enzyme was sensitive to catabolite repression. The other enzymes of the arginine dihydrolase pathway, namely, ornithine carbamoyl-transferase and carbamate kinase, did not show such variation.
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bacteriology
دوره 91 1 شماره
صفحات -
تاریخ انتشار 1966