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Superoxide dismutase properties

Structure and Properties of Copper-Zinc Superoxide Dismutases Ivano Bertini, Stefano Mangani, and Maria Silvia Viezzoli... [Pg.514]

It is possible that dietary flavonoids participate in the regulation of cellular function independent of their antioxidant properties. Other non-antioxidant direct effects reported include inhibition of prooxidant enzymes (xanthine oxidase, NAD(P)H oxidase, lipoxygenases), induction of antioxidant enzymes (superoxide dismutase, gluthathione peroxidase, glutathione S-transferase), and inhibition of redox-sensitive transcription factors. [Pg.138]

J.A. Fee and R.G. Briggs, Reconstitution of bovine erythrocyte superoxide dismutase. V. Preparation and properties of derivatives in which both zinc and copper sites contain copper. Biochim. Biophy. Acta. 400, 439 150 (1975). [Pg.205]

J.A. Fee and P.E. DiCorleto, Oxidation-reduction properties of bovine erythrocyte superoxide dismutase. Biochemistry. 12, 4893-4899 (1973). [Pg.206]

F. Yamakura, K. Kobayashi, H. Ue, and M. Konno, The pH-dependent changes of the enzymic activity and spectroscopic properties of iron-substituted manganese superoxide dismutase. A study on the metal-specific activity of Mn-containing superoxide dismutase. Eur. J. Biochem. 227, 700—706 (1995). [Pg.207]

The antioxidant system in humans is a complex network composed by several enzymatic and nonenzymatic antioxidants. In addition to being an antioxidant, lycopene also exerts indirect antioxidant properties by inducing the production of cellular enzymes such as superoxide dismutase, glutathione S-transferase, and quinone reductase that also protect cells from reactive oxygen species and other electrophilic molecules (Goo and others 2007). [Pg.207]

Bruijn, L. I., Beal, M. F., Becher, M. W. et al. Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. Proc. Natl Acad. Sci. U.S.A. 94 7606-7611,1997. [Pg.743]

This discussion of copper-containing enzymes has focused on structure and function information for Type I blue copper proteins azurin and plastocyanin, Type III hemocyanin, and Type II superoxide dismutase s structure and mechanism of activity. Information on spectral properties for some metalloproteins and their model compounds has been included in Tables 5.2, 5.3, and 5.7. One model system for Type I copper proteins39 and one for Type II centers40 have been discussed. Many others can be found in the literature. A more complete discussion, including mechanistic detail, about hemocyanin and tyrosinase model systems has been included. Models for the blue copper oxidases laccase and ascorbate oxidases have not been discussed. Students are referred to the references listed in the reference section for discussion of some other model systems. Many more are to be found in literature searches.50... [Pg.228]

Ali SS, Hardt JI, Quick KL, Kim-Han JS, Erlanger BF, Huang TT, Epstein CJ, Dugan LL (2004) A biologically effective fullerene (C60) derivative with superoxide dismutase mimetic properties. Free Rad. Biol. Med. 37 1191-1202. [Pg.17]

Higashi N, Shosu T, Koga T, Niwa M, Tanigawa T (2006) pH-responsive, self-assembling nanoparticle from a fullerene-tagged poly(L-glutamic acid) and its superoxide dismutase mimetic property. J. Colloid Interface Sci. 298 118-123. [Pg.18]


See other pages where Superoxide dismutase properties is mentioned: [Pg.492]    [Pg.170]    [Pg.124]    [Pg.309]    [Pg.45]    [Pg.114]    [Pg.363]    [Pg.247]    [Pg.200]    [Pg.207]    [Pg.293]    [Pg.201]    [Pg.319]    [Pg.170]    [Pg.64]    [Pg.309]    [Pg.364]    [Pg.133]    [Pg.278]    [Pg.90]    [Pg.120]    [Pg.97]    [Pg.70]    [Pg.535]    [Pg.588]    [Pg.147]    [Pg.80]    [Pg.167]    [Pg.74]   
See also in sourсe #XX -- [ Pg.33 , Pg.199 ]

See also in sourсe #XX -- [ Pg.199 ]




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