The reduction of nicotinamide N-oxide by xanthine oxidase.

نویسندگان

  • K N Murray
  • S Chaykin
چکیده

The following evidence has led to the conclusion that xanthine oxidase, with its usual electron donors, is capable of reducing nicotinamide N-oxide to nicotinamide. 1. The purest enzyme fraction from hog liver which catalyzes the reduction has the spectrum of a metalloflavoprotein and has xanthine oxidase activity. 2. The enzyme responsible for the reduction cofractionates with hog liver xanthine oxidase. 33 Milk xanthine oxidase also catalyzes the reduction of nicotinamide N-oxide. 4. The electron donors for the reduction are known substrates of xanthine oxidase. 5. Both milk and liver xanthine oxidases exhibit separate pH optima for the reductions dependent on reduced diphosphopyridine nucleotide and xanthine. 6. Xanthine oxidase activity and nicotinamide N-oxide reduction activity are destroyed by heat at the same rate. 7. Each activity decreases to the same extent in the livers of rats maintained on protein-deficient diets. 8. Xanthine oxidase activity and xanthine-dependent nicotinamide N-oxide reduction exhibit parallel inhibition by cyanide. It is proposed that xanthine oxidase might be responsible for other N-oxide reductions.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Loss of fluorescence by anthracycline antibiotics: effects of xanthine oxidase and identification of the nonfluorescent metabolites.

Rat liver cytosol and buttermilk xanthine oxidase both converted 7-deoxypyrromycinone, the 7-deoxyaglycone of marcellomycin, a new anthracycline antibiotic, to a nonfluorescent compound under anaerobic conditions and in the presence of an electron donor. Reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate were equally effective electron donors for l...

متن کامل

Onion, a Potent Inhibitor of Xantine Oxidase

Onion (Allium Cepa) contains high levels of flavonoids. Although there are many studies indicating the inhibitory effects of flavonoids on xanthine oxidase, there is no report on the effect of onion on this enzyme. Therefore, in the present study, the inhibitory effects of onion on xanthine oxidase are investigated. Fresh filtered juice of onion was prepared and its inhibitory effect on guine...

متن کامل

Reduction of epoxy derivatives of benzo(a)pyrene by microsomal cytochrome P-450.

Benzo(a)pyrene 4,5-oxide was rapidly reduced to benzo(a)pyrene by rat liver microsomes in the presence of reduced nicotinamide adenine dinucleotide phosphate when incubated anaerobically. The activity of benzo(a)pyrene 4,5oxide reductase was increased about seven times by pretreat ment of rats with 3-methylcholanthrene. The addition of riboflavin to the incubation mixture resulted in the increa...

متن کامل

Reduction of Epoxy Derivatives of Benzo(a)pyrene by Microsomal Cytochrome P-4501

Benzo(a)pyrene 4,5-oxide was rapidly reduced to benzo(a)pyrene by rat liver microsomes in the presence of reduced nicotinamide adenine dinucleotide phosphate when incubated anaerobically. The activity of benzo(a)pyrene 4,5oxide reductase was increased about seven times by pretreat ment of rats with 3-methylcholanthrene. The addition of riboflavin to the incubation mixture resulted in the increa...

متن کامل

Microbial degradation of corrinoids. VI. Reduction of hydroxocobalamin by cell-free particles from Pseudomonas rubescens.

Cell-free particles from Pseudomonas rubescens have been shown to reduce hydroxocobalamin to vitamin B(12r). The particles are unable to reduce the B(12r) to B(12s). The reduction of hydroxocobalamin is dependent upon reduced nicotinamide adenine dinucleotide and is stimulated by flavin adenine dinucleotide. Cobinamide and diaquocobinamide were reduced at 25 and 10%, respectively, of the rate o...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 241 15  شماره 

صفحات  -

تاریخ انتشار 1966