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Clostridium purinolyticum

Durre P, JR Andreesen (1982) Anaerobic degradation of uric acid via pyrimidine derivatives by selenium-starved cells of Clostridium purinolyticum. Arch Microbiol 131 255-260. [Pg.548]

Self WT, TC Stadman (2000) Selenium-dependent metabolism of purines a selenium-dependent purine hydroxylase and xanthine dehydrogenase were purified from Clostridium purinolyticum and characterized. Proc Natl Acad Sci USA 97 7208-7213. [Pg.552]

Xanthine dehydrogenase of Clostridium purinolyticum, Clostridium acidiurici, and... [Pg.121]

Dtlrre P, Andersch W, Andreesen JR. 1981. Isolation and characterization of an adenine-utilizing, anaerobic sporeformer, Clostridium purinolyticum sp. nov. Int J Syst Bacteriol 31 184-94. [Pg.168]

Garcia GE, Stadtman TC. 1991. Selenoprotein A component of the glycine rednctase complex from Clostridium purinolyticum nucleotide sequence of the gene shows that selenocysteine is encoded by UGA. J Bacteriol 173 2093-8. [Pg.169]

Sliwkowski MX, StadtmanTC. 1988. Selenium-dependent glycine reductase differences in physicochemical properties and biological activities of selenoprotein A components isolated from Clostridium sticklandii and Clostridium purinolyticum. Biofactors 1 293-6. [Pg.169]

Figure 3.5 Plots of the -values of Mo(v) species against g -anisotropy for members of the XO enzymes family. In red, slow-type signals from Dg AOR slow-type aquo from milk XO (2), with %poxanthine from Clostridium purinolyticum Purine Hydroxylase (3). In black, rapid-type signal from milk XO (4), rapid q from Pseudomonas putida Quinoline 2-Oxidore-ductase (5), rapid type 1 with 1-methybcanthine from milk XO (6), Thauera aromatica 4-Hydroxybenzoyl-CoA reductase (7), rapid q from As QualOx (8), rapid type 2 borate from milk XO (9), resting q2 from Pp QuinOr (10), rapid q from Pd IsoOr (11), resting q from Pp QuinOr (12). In blue, very rapid-type signals from Pp QuinOr (13), with 2-Hydroxy-6-methylpurine from milk XO (14)," from Pd IsoOr (15), from As QualOx (16). Linear correlations between the available data sets within each family can be extrapolated and are schematically indicated by straight lines to help the reader. Figure 3.5 Plots of the -values of Mo(v) species against g -anisotropy for members of the XO enzymes family. In red, slow-type signals from Dg AOR slow-type aquo from milk XO (2), with %poxanthine from Clostridium purinolyticum Purine Hydroxylase (3). In black, rapid-type signal from milk XO (4), rapid q from Pseudomonas putida Quinoline 2-Oxidore-ductase (5), rapid type 1 with 1-methybcanthine from milk XO (6), Thauera aromatica 4-Hydroxybenzoyl-CoA reductase (7), rapid q from As QualOx (8), rapid type 2 borate from milk XO (9), resting q2 from Pp QuinOr (10), rapid q from Pd IsoOr (11), resting q from Pp QuinOr (12). In blue, very rapid-type signals from Pp QuinOr (13), with 2-Hydroxy-6-methylpurine from milk XO (14)," from Pd IsoOr (15), from As QualOx (16). Linear correlations between the available data sets within each family can be extrapolated and are schematically indicated by straight lines to help the reader.
See other pages where Clostridium purinolyticum is mentioned: [Pg.130]    [Pg.130]    [Pg.121]    [Pg.131]    [Pg.141]    [Pg.130]    [Pg.130]    [Pg.121]    [Pg.131]    [Pg.141]    [Pg.160]   
See also in sourсe #XX -- [ Pg.158 , Pg.160 , Pg.165 , Pg.166 ]



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