Variation in glucose-6-phosphate dehydrogenase in relation to the growth phase and frequency of sex chromatin positive cells in cultures of fibroblasts from normal human females and a 48-XXXY male

A highly sensitive cytochemical method for the assay of the ability of plasma and extracts of human urine to stimulate renal glucose-6-phosphate dehydrogenase (G6PD) activity in vitro is described. In the proximal convoluted tubules there was a linear increase of G6PD activity with the logarithm of concentration of a highly purified natriuretic extract from normal human urine (0·384–384 ng active material/l) which was used as a standard. The stimulation of G6PD obtained with dilutions of normal human plasma was parallel to that produced by the standard. The sensitivity of the assay permitted the measurement of as little as 0·384 ng active material/l of the natriuretic extract (0·001 units/ml) and dilutions of 1/10 000 could be detected using normal human plasma. The mean ± s.e.m. index of precision was 0·068± 0·003 (n = 9). It is known that inhibition of sodium potassium-dependent adenosine triphosphatase (Na+-K+-ATPase) is associated with a rise in G6PD activity. We have confirmed this observation by demonstrating that ouabain, a potent inhibitor of Na+ -K+-ATPase, stimulates renal G6PD activity in our assay and that natriuretic extract, human plasma and ouabain stimulated renal G6PD activity in vitro and simultaneously inhibited renal Na+-K+-ATPase activity in vitro. The plasma from 12 normal subjects (five of whom were previously shown to inhibit renal Na+-K+-ATPase activity in vitro in a manner related to sodium intake) stimulated renal G6PD activity in vitro, and this activity was also directly related to sodium intake. It is suggested that the change in the capacity of plasma to stimulate renal G6PD activity in vitro is a marker of the concentration of a circulating sodium transport inhibitor.

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Pregnancy-Induced Changes in Rat Tissue Glucose-6-Phosphate Dehydrogenase Activities and Sex Chromatin Frequencies

Biology of Reproduction ◽

10.1095/biolreprod1.2.157 ◽

1969 ◽

Vol 1 (2) ◽

pp. 157-166 ◽

Cited By ~ 1

Author(s):

J. STEWART

Keyword(s):

Sex Chromatin ◽

Rat Tissue ◽

Induced Changes ◽

Glucose 6 Phosphate Dehydrogenase

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The toxic action of phenothiazine and some disturbances of intermediary metabolism in undernourished sheep

Australian Journal of Agricultural Research ◽

10.1071/ar9630529 ◽

1963 ◽

Vol 14 (4) ◽

pp. 529 ◽

Cited By ~ 4

Author(s):

JH Koch

Keyword(s):

Oxidative Phosphorylation ◽

Liver Mitochondria ◽

Weight Losses ◽

Loss Of Weight ◽

Quality Diet ◽

Fatty Livers ◽

Normal Human ◽

Uncoupling Of Oxidative Phosphorylation ◽

Glucose 6 Phosphate Dehydrogenase ◽

Considerable Loss

Uncoupling of oxidative phosphorylation was found in preparations of liver mitochondria obtained from adequately fed sheep, killed 24 hr after the administration of phenothiazine. Sheep fed a low quality diet suffered considerable loss of weight and all had fatty livers at necropsy. The extent of the fatty change seemed to be related to the rate of weight loss. Liver mitochondria from sheep which had lost body weight at an average of 0.3 lb/day had normal biochemical activities. The administration of phenothiazine to such sheep caused uncoupling of oxidative phosphorylation. Animals with weight losses of 0.33 lb day or more showed depressed mitochondria] respiration rates with very little phosphorylation. Phenothiazine did not increase the Q(N)O2 values in such sheep. Glucose 6-phosphate dehydrogenase activity was found to be extremely low in sheep erythrocytes—approximately 5% of normal human red cell values. The activity of this enzyme was not affected by malnutrition, or by phenothiazine administration to either well-fed or undernourished sheep.

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SEX-CHROMATIN BODY IN NORMAL HUMAN TESTIS

The Lancet ◽

10.1016/s0140-6736(61)92121-3 ◽

1961 ◽

Vol 277 (7168) ◽

pp. 79-80 ◽

Cited By ~ 15

Author(s):

J.S.S. Stewart ◽

AnnR. Sanderson

Keyword(s):

Human Testis ◽

Sex Chromatin ◽

Chromatin Body ◽

Normal Human

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The Regeneration of Reduced Glutathione in Normal and Glucose-6-Phosphate Dehydrogenase Deficient Human Red Blood Cells

Blood ◽

10.1182/blood.v29.3.313.313 ◽

1967 ◽

Vol 29 (3) ◽

pp. 313-319 ◽

Cited By ~ 45

Author(s):

NECHAMA S. KOSOWER ◽

GRACE A. VANDERHOFF ◽

IRVING M. LONDON

Keyword(s):

Red Blood Cells ◽

Blood Cells ◽

Reduced Glutathione ◽

Rapid Rate ◽

Oxidizing Agent ◽

Human Red Blood Cells ◽

Normal Human ◽

Glucose 6 Phosphate Dehydrogenase ◽

Gssg Reductase ◽

Normal Erythrocyte

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.

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