A kinetic study of pig liver glucose dehydrogenase

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

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 - Jan 1 1976

Fingerprint

Glucose 1-Dehydrogenase
L-fucose dehydrogenase
NADP
Liver
NAD
Swine
Arabinose
Kinetics
Xylose
Substrates
Glucagon
Insulin
Glucose
beta-glucono-1,5-lactone
xylose-glucose
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A kinetic study of pig liver glucose dehydrogenase. / Carper, W. Robert; Toews, Myron Lee; Thompson, Richard E.; Buess, Charles M.

In: Archives of Biochemistry and Biophysics, Vol. 175, No. 1, 01.01.1976, p. 312-320.

Research output: Contribution to journalArticle

Carper, W. Robert ; Toews, Myron Lee ; Thompson, Richard E. ; Buess, Charles M. / A kinetic study of pig liver glucose dehydrogenase. In: Archives of Biochemistry and Biophysics. 1976 ; Vol. 175, No. 1. pp. 312-320.
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