Glucose 6 phosphate dehydrogenase. Purification and partial characterization

M. I. Kanji, Myron Lee Toews, W. R. Carper

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

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
Volume251
Issue number8
StatePublished - Dec 1 1976

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Glucose-6-Phosphate
Glucosephosphate Dehydrogenase
NADP
Purification
Molecular Weight
Molecular weight
Enzymes
Ionic strength
Dimers
Liver
Osmolar Concentration
Cytoplasm
Swine
Monomers

ASJC Scopus subject areas

  • Biochemistry

Cite this

Glucose 6 phosphate dehydrogenase. Purification and partial characterization. / Kanji, M. I.; Toews, Myron Lee; Carper, W. R.

In: Journal of Biological Chemistry, Vol. 251, No. 8, 01.12.1976, p. 2255-2257.

Research output: Contribution to journalArticle

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