A kinetic study of pig liver glucose dehydrogenase

W. Robert Carper, Myron L. Toews, Richard E. Thompson, Charles M. Buess

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

The steady state kinetics of pig liver glucose dehydrogenase with NAD, NADP, d-glucose, and d-xylose as substrates is reported. Alternate substrate, product inhibition, and dead-end inhibition studies support an ordered Bi Bi mechanism as is the case with arabinose (fucose) dehydrogenase from the same source. Only NADH acts as an inhibitor, whereas NADPH, xylolactone, and gluconolactone exhibit no product inhibition. Insulin and glucagon have no effect on glucose dehydrogenase kinetics in vitro.

Original languageEnglish (US)
Pages (from-to)312-320
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume175
Issue number1
DOIs
StatePublished - Jul 1976
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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