Excess substrate inhibition of xanthine oxidase: a reexamination.
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.
Hausladen
A
A
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.
Fridovich
I
I
D000818:Animals; D001462:Barbital / Q000494:pharmacology; D002021:Buffers; D002417:Cattle; D005260:Female; D005998:Glycine / Q000031:analogs & derivatives / Q000494:pharmacology; D007700:Kinetics; D008433:Mathematics; D008892:Milk / Q000201:enzymology; D010710:Phosphates / Q000494:pharmacology; D017680:Potassium Compounds / Q000494:pharmacology; D012044:Regression Analysis; D014325:Tromethamine / Q000494:pharmacology; D019820:Xanthine; D014969:Xanthine Oxidase / Q000037:antagonists & inhibitors*; D014970:Xanthines / Q000494:pharmacology*
D002021:Buffers; D010710:Phosphates; D017680:Potassium Compounds; D014970:Xanthines; D014325:Tromethamine; D019820:Xanthine; C027494:N,N-bis(2-hydroxyethyl)glycine; D001462:Barbital; C013216:potassium phosphate; D014969:Xanthine Oxidase; D005998:Glycine