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Excess substrate inhibition of xanthine oxidase: a reexamination
1Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.
Archives of Biochemistry and Biophysics
|November 1, 1993
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.