Abstract
Xanthine oxidase has long been considered to be subject to inhibition by excess substrate. It is now shown that, although such inhibition can be seen in Tris or N,N-bis(2-hydroxyethyl)glycine buffers, earlier reports in which phosphate, pyrophosphate, or Veronal buffers were used were probably the result of a spectrophotometric artifact imposed by stray light in the incident beam.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Barbital / pharmacology
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Buffers
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Cattle
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Female
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Glycine / analogs & derivatives
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Glycine / pharmacology
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Kinetics
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Mathematics
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Milk / enzymology
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Phosphates / pharmacology
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Potassium Compounds / pharmacology
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Regression Analysis
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Tromethamine / pharmacology
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Xanthine
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Xanthine Oxidase / antagonists & inhibitors*
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Xanthines / pharmacology*
Substances
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Buffers
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Phosphates
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Potassium Compounds
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Xanthines
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Tromethamine
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Xanthine
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N,N-bis(2-hydroxyethyl)glycine
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Barbital
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potassium phosphate
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Xanthine Oxidase
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Glycine