scholarly journals Noninferiority of glucose-6-phosphate dehydrogenase deficiency diagnosis by a point-of-care rapid test vs the laboratory fluorescent spot test demonstrated by copper inhibition in normal human red blood cells

2015 ◽  
Vol 165 (6) ◽  
pp. 677-688 ◽  
Author(s):  
J. Kevin Baird ◽  
Mewahyu Dewi ◽  
Decy Subekti ◽  
Iqbal Elyazar ◽  
Ari W. Satyagraha
Blood ◽  
1967 ◽  
Vol 29 (3) ◽  
pp. 313-319 ◽  
Author(s):  
NECHAMA S. KOSOWER ◽  
GRACE A. VANDERHOFF ◽  
IRVING M. LONDON

Abstract Reduced glutathione (GSH) was rapidly regenerated in normal human red blood cells treated with the GSH oxidizing agent, methyl phenylazoformate. Erythrocytes of G-6-PD deficient males regenerated little, if any, GSH under the same conditions. The rate of regeneration of GSH in erythrocytes of G-6-PD deficient heterozygote females was similar to that of a mixture of normal red blood cells and erythrocytes of G-6-PD deficient males. It was compatible with the assumption of mosaicism of the erythrocytes in the heterozygote females. The rapid rate at which the normal erythrocyte can regenerate its GSH may render it capable of continuously absorbing free radicals derived from drugs without harmful consequences to the cell. Study of the rate of regeneration of GSH in erythrocytes treated with methyl phenylazoformate may be useful in the detection of deficiencies of G-6-PD, GSSG reductase, and hexokinase.


1985 ◽  
Vol 152 (1-2) ◽  
pp. 135-142 ◽  
Author(s):  
E. Solem ◽  
C. Pirzer ◽  
M. Siege ◽  
F. Kollmann ◽  
O. Romero-Saravia ◽  
...  

1976 ◽  
Vol 128 (2) ◽  
pp. 184-187 ◽  
Author(s):  
Helen L. White ◽  
Malcolm N. McLeod ◽  
Jonathan R. T. Davidson

SummaryCatechol O-methyltransferase of lysed human red blood cells was assayed under optimal conditions, using saturating concentrations of the substrates, S-adenosyl-L-methionine and 3,4-dihydroxybenzoic acid. The mean enzyme activity found in 24 normal subjects was 29.2 nmol/hr/ml RBC. The mean activity in blood of 33 female unipolar depressives was not significantly different from normal. However, higher enzyme activities were observed in the blood of 11 schizophrenic patients (38.9 nmol/hr/ml RBC). Partially purified enzyme preparations from blood of normal and schizophrenic individuals were indistinguishable with respect to substrate specificities, isoelectric pH values, and ratios of the two O-methylated products. Therefore it is unlikely that any defect in O-methylation which may occur in schizophrenia can be attributed to a change in the intrinsic properties of erythrocyte catechol O-methyltransferase.


2007 ◽  
Vol 41 (5) ◽  
pp. 536-545 ◽  
Author(s):  
Irina M. Shcherbachenko ◽  
Irina L. Lisovskaya ◽  
Vladimir P. Tikhonov

Nature ◽  
1962 ◽  
Vol 195 (4840) ◽  
pp. 500-501 ◽  
Author(s):  
ROBERT H. HERMAN ◽  
JESSE BERKOWITZ ◽  
LLOYD E. CLAYTON ◽  
JACQUES L. SHERMAN

2012 ◽  
Vol 88 (1) ◽  
pp. 44-51 ◽  
Author(s):  
Robert S. Franco ◽  
M. Estela Puchulu-Campanella ◽  
Latorya A. Barber ◽  
Mary B. Palascak ◽  
Clinton H. Joiner ◽  
...  

Enzyme ◽  
1988 ◽  
Vol 39 (1) ◽  
pp. 1-7 ◽  
Author(s):  
J. L. Vives Carrons ◽  
M. A. Pujades ◽  
D. Colomer

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