Frequency of Glutathione Reductase, Pyruvate Kinase and Glucose-6-Phosphate Dehydrogenase Deficiency in a Spanish Population

1979 ◽  
Vol 29 (5) ◽  
pp. 310-313 ◽  
Author(s):  
Carmona García ◽  
Casado Moragón ◽  
M.E. López-Fernández
Blood ◽  
1966 ◽  
Vol 28 (6) ◽  
pp. 942-942
Author(s):  
ERNEST BEUTLER ◽  
Agnes Halasz

Abstract BEUTLER, E.: A SERIES OF NEW SCREENING PROCEDURES FOR PYRUVATE KINASE DEFICIENCY, GLUCOSE-6-PHOSPHATE DEHYDROGENASE DEFICIENCY, AND GLUTATHIONE REDUCTASE DEFICIENCY. Blood 28:553-562, 1966. In the October 1966 issue of Blood, on page 557 the concentration for GSSG was erroneously given as .003 M. The line under B. Reaction Mixture should read: GSSG, .033M 0.1 ml.


Blood ◽  
1966 ◽  
Vol 28 (4) ◽  
pp. 553-562 ◽  
Author(s):  
ERNEST BEUTLER ◽  
Agnes Halasz

Abstract A new type of screening procedure for the detection of enzymatic defects of the red cell has been described. The blood or red cell sample is added to the reaction mixture. After a suitable period of incubation a drop of the mixture is spotted on filter paper, permitted to dry, and examined for fluorescence under UV light. In this way the oxidation of reduction of pyridine nucleotides is readily evaluated. Reaction mixtures for the detection of glucose-6-phosphate dehydrogenase deficiency, pyruvate kinase deficiency, and glutathione reductase deficiency are described. The same general procedure should be readily adaptable to the detection of other enzymatic deficiencies of red cells, such as phosphogluconate dehydrogenase deficiency or triosephosphate isomerase deficiency.


1969 ◽  
Vol 114 (4) ◽  
pp. 833-837 ◽  
Author(s):  
Satish K. Srivastava ◽  
Ernest Beutler

1. Erythrocytes from normal and glucose 6-phosphate dehydrogenase-deficient humans were subjected to hydrogen peroxide diffusion to oxidize the GSH. Studies were carried out in the presence and absence of chromate to inhibit glutathione reductase and with or without the addition of glucose. 2. The GSH content of erythrocytes from other species was oxidized by subjecting them to hydrogen peroxide diffusion in the presence of chromate and glucose. 3. Chromate (1·3mm) inhibited glutathione reductase by about 80%, whereas glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, hexokinase, phosphofructokinase and pyruvate kinase were not inhibited. 4. The GSSG formed was transported from the erythrocytes to the medium. 5. The transport rate of GSSG from glucose 6-phosphate dehydrogenase-deficient erythrocytes subjected to hydrogen peroxide diffusion in the presence of chromate was comparable with that from normal and glucose 6-phosphate dehydrogenase-deficient erythrocytes. 6. The rate of transport of GSSG from erythrocytes of various species studied could be ranked: pigeon>rabbit>rat>donkey>man>dog>horse>sheep>chicken>fish.


Author(s):  
O.Yu. Kushnir ◽  
I.M. Yaremii

The increasing incidence of type 1 diabetes coupled with advances in treatment of type 1 diabetes has resulted in an unprecedented number of older adults living with and controllable type 1 diabetes. The objective of this experimental study was to assess the impact of aging on the level of basal glycaemia and activities of glucose-6-phosphate dehydrogenase [EC1.1.1.49], pyruvate kinase [EC 2.7.1.40] and glutathione reductase [EC1.6.4.2] in erythrocytes of alloxan-diabetic rats. Methods: We used 100 male Wistar rats, divided into two age groups: I group included- 2-month (adult) animals, and II group was made up of 4-month (old) animals. Diabetes was modelled by injecting the rats with 5% solution of alloxan monohydrate intraperitoneally in a dose of 170 mg/kg. Blood was taken from the tail vein to evaluate the basal glycaemia on 5-th and 47-th day after the alloxan injection. Rats were sacrificed on the 47-th day of the experiment in accordance with the regulations on ethical treatment of vertebrates. The assessment of the activity of the enzymes was carried out by standard methods. Statistical analysis was performed by using Statistica 10 StatSoft Inc. Results. The level of basal glycaemia on the fifth day of the experiment in the animals of both groups went up on average by 115% from baseline values. We founded that on 47-th day this index was higher in group of old rats by 20% than in adult rats. Pyruvate kinase activity in erythrocytes of adult and old animals with diabetes decreased by 35% and 50% respectively compared with the control. Glucose-6-phosphate dehydrogenase activity in erythrocytes of adult and old animals with diabetes decreased by 27% and 45% respectively compared with the control on 47-th day. The changes may be considered as the result of age-related disorders of glucose metabolism due to disturbances in free radical mechanisms. Glutathione reductase activity in erythrocytes of adult and old animals with diabetes decreased by 29% and 35% respectively compared with the control on 47-th day. Conclusion. We have determined when getting aged, the alloxan-diabetic rats demonstrate changes in the sensitivity of pyruvate kinase, glucose-6-phosphate dehydrogenase and glutathione reductase activities in erythrocytes resulted from the effect of diabetes mellitus factors (hyperglycaemia). We can suggest that glycaemic control is key purpose for older patients with type 1 diabetes in order to prevent of complication, which can be aggravated with age.


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