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

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

doi:10.1016/0304-4165(91)90046-J

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

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

A.O.U. San Martino - IST, Istituto Nazionale Ricerca sul Cancro (GENOVA)

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	101-104
Number of pages	4
Journal	BBA - General Subjects
Volume	1074
Issue number	1
DOIs	https://doi.org/10.1016/0304-4165(91)90046-J
Publication status	Published - May 24 1991

Keywords

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

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/0304-4165(91)90046-J

Cite this

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title = "Bound and unbound pyridine dinucleotides in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes",

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.",

keywords = "(Human erythrocyte), Glucose-6-phosphate dehydrogenase, NAD(H), NADP(H)",

author = "Letizia Canepa and Ferraris, {Anna Maria} and Maurizio Miglino and Gaetani, {Gian Franco}",

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T1 - Bound and unbound pyridine dinucleotides in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes

AU - Canepa, Letizia

AU - Ferraris, Anna Maria

AU - Miglino, Maurizio

AU - Gaetani, Gian Franco

PY - 1991/5/24

Y1 - 1991/5/24

N2 - 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.

AB - 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.

KW - (Human erythrocyte)

KW - Glucose-6-phosphate dehydrogenase

KW - NAD(H)

KW - NADP(H)

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

Abstract

Keywords

ASJC Scopus subject areas

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