Properties of hepatic hexose-6-phosphate dehydrogenase purified from brook trout and lake trout

John J. Stegeman*, Erwin Goldberg

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

1. 1. Brook trout hexose-6-phosphate dehydrogenase (H6PD) and lake trout H6PD are essentially identical in several parameters including pH optima, kinetic properties and activation energy. They differ in thermal stability. 2. 2. The various oxidations catalyzed by trout H6PD differ in their response to the presence of Mg2+, ATP and several anions. 3. 3. The apparent Km's of all four substrates show a decrease with decreasing temperature. 4. 4. Kinetics of substrate oxidation by H6PD suggest that the enzyme most likely functions as a G6PD.

Original languageEnglish (US)
Pages (from-to)241-256
Number of pages16
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume43
Issue number2
DOIs
StatePublished - Oct 15 1972

Keywords

  • ATP
  • Glucose-6-phosphate dehydrogenase
  • Mg
  • Salvelinus fontinalis
  • Salvelinus namaycush
  • acclimation
  • activation energy
  • anions
  • brook trout
  • enzyme inhibition
  • enzyme kinetics
  • enzyme stimulation
  • hexose-6-phosphate dehydrogenase
  • isoelectric point
  • lake trout
  • pH optima
  • salmonids
  • thermal denaturation

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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