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 | |
| Publication status | Published - 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
Cite this
Bound and unbound pyridine dinucleotides in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes. / Canepa, Letizia; Ferraris, Anna Maria; Miglino, Maurizio; Gaetani, Gian Franco.
In: BBA - General Subjects, Vol. 1074, No. 1, 24.05.1991, p. 101-104.Research output: Contribution to journal › Article
}
TY - JOUR
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)
UR - http://www.scopus.com/inward/record.url?scp=0025863168&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025863168&partnerID=8YFLogxK
U2 - 10.1016/0304-4165(91)90046-J
DO - 10.1016/0304-4165(91)90046-J
M3 - Article
VL - 1074
SP - 101
EP - 104
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
SN - 0304-4165
IS - 1
ER -