Glucose 6 phosphate dehydrogenase. Purification and partial characterization

M. I. Kanji, M. L. Toews, W. R. Carper

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Glucose 6 phosphate dehydrogenase has been purified 1000 fold from pig liver. This enzyme exists as an active dimer of molecular weight 133,000 and an inactive monomer of molecular weight 67,500. The pH of maximum activity is 8.5 and the ionic strength maximum is 0.1 to 0.5 M. Glucose 6 phosphate dehydrogenase is highly specific for NADP+ and glucose 6 phosphate. Apparent K(m) values of 3.6 μM and 5.4 μM were obtained for glucose 6 phosphate and NADP+. This enzyme is located almost entirely within the soluble portion of the cellular cytoplasm.

Original languageEnglish (US)
Pages (from-to)2255-2257
Number of pages3
JournalJournal of Biological Chemistry
Issue number8
StatePublished - 1976
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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