Bound and unbound pyridine dinucleotides in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes

Letizia Canepa, Anna Maria Ferraris, Maurizio Miglino, Gian Franco Gaetani

Research output: Contribution to journalArticle

Abstract

We have measured, by a sensitive cycling assay, the concentration of bound and unbound dinucleotides in normal and glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes. Measurement of free NADP in ultrafiltrates confirms that in normal erythrocytes almost all NADP is bound to cytosolic proteins. In glucose-6-phosphate dehydrogenase-deficient erythrocytes unbound NADP is significantly higher than in normal red cells and the NADP+/NADPH ratio is largely in favor of the oxidized form. In normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes essentially all NAD (bound and unbound) is in the oxidized state. About 50% of the total amount of NAD (NAD+ + NADH) is free in the cytosol, with a NAD+/NADH ratio greater than 100.

Original languageEnglish
Pages (from-to)101-104
Number of pages4
JournalBBA - General Subjects
Volume1074
Issue number1
DOIs
Publication statusPublished - May 24 1991

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Keywords

  • (Human erythrocyte)
  • Glucose-6-phosphate dehydrogenase
  • NAD(H)
  • NADP(H)

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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