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- W2435255514 abstract "The desulfo form of milk xanthine oxidase (xan- thine:oxygen oxidoreductase, EC 1.2.3.2) was reactivated by in- cubation with rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1), thiosulfate, and sulfhydryl reagent; 50% of full ac- tivity was recovered. No further reactivation occurred with ad- ditional incubation. It was also found that .native enzyme, in. the sulfo form with full activity was inactivated by incubation with the same system, down to half of full activity and no further inacti- vation occurred. After these incubations the enzyme was found to be a mixture of functional and nonfunctional enzymes based on spectral changes with xanthine, on (4C)oxipurinol equilibration, and on steady-state kinetics. The 35S of (35S)thiosulfate was in- corporated into desulfo xanthine oxidase in -parallel with an in- crease in catalytic activity. Most of the 35S was cyanolysable but was protected from cyanolysis by pretreatment with allopurinol. The 35S was released from 35S-labeled reconstituted xanthine ox- idase upon incubation with the rhodanese system .containing un- labeled thiosulfate. However, catalytic activity remained un- changed, indicating that the sulfur atom was exchanged during the incubation." @default.
- W2435255514 created "2016-06-24" @default.
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- W2435255514 date "2016-01-01" @default.
- W2435255514 modified "2023-09-27" @default.
- W2435255514 title "Reversible interconversion betweel oxidase in a system containing rho( sulfhydryl reagent (sulfuration/desulfuration)." @default.
- W2435255514 hasPublicationYear "2016" @default.
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