Isoenzyme polymorphism of 6-phosphogluconate dehydrogenase (EC 1.1.1.44) in the family Equidae

Isoenzymes of 6-PGD were investigated in three Equidae species. In this family the enzyme 6-PGD is controlled by one autosomal gene locus with differential allele frequencies occurring in the horse, mule and donkey.     

The determination of the red cell isoenzymes 6-phosphogluconate dehydrogenase (E.C.1.1.1.44) and acid phosphatase (E.C.3.1.3.2) by means of agarosegel thinlayer electrophoresis (author's transl)

Methods for the determination of the red cell isoenzymes 6-PGD and acP by means of agarosegel thinlayer electrophoresis are referred. Using these relatively simple techniques, results can be obtained after at least two hours. The quality of separation in both systems is higher than that obtained after starch gel electrophoresis.     

X-linked glucose-6-phosphate dehydrogenase (G6PD) and autosomal 6-phosphogluconate dehydrogenase (6PGD) polymorphisms in baboons

Electrophoretic polymorphisms of glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) were examined in captive colonies of five subspecies of baboons (Papio hamadryas). Phenotype frequencies and family data verified the X-linked inheritance of the G6PD polymorphism. Insufficient family data were available to confirm autosomal inheritance of the 6PGD polymorphism, but the electrophoretic patterns of variant types (putative heterozygotes) suggested the codominant expression of alleles at an autosomal locus. Implications of the G6PD polymorphism are discussed with regard to its utility as a marker system for research on X-chromosome inactivation during baboon development and for studies of clonal cell proliferation and/or cell selection during the development of atherosclerotic lesions in the baboon model.     

Effects of some drugs on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro study

Inhibitory effects of some drugs were investigated on human erythrocyte 6-phosphogluconate dehydrogenase obtained with a 6552-fold purification in a yield of 78% using 2′, 5′-ADP Separose 4B affinity gel. Which on SDS polyacrylamide gel electrophoresis showed a single band. Larnoxicam, metronidazole, imipenem, ornidazole, vancomycin, clindamycin, and amoxicillin exhibited inhibitory effects on the enzyme in vitro with IC₅₀ values of 0.17, 0.23, 0.43, 21.79, 46.39, 117.43 and 287.35 mM, and the Ki constants 0.40 ± 0.04, 0.57 ± 0.06, 0.77 ± 0.11, 42.40 ± 2.89, 65.60 ± 4.03, 130.22 ± 9.21, and 287.58 ± 10.56 mM, respectively. While vancomycin, clindamycin and amoxicillin showed competitive inhibition the other drugs displayed noncompetitive inhibition.     

Effects of some drugs on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro study

Inhibitory effects of some drugs were investigated on human erythrocyte 6-phosphogluconate dehydrogenase obtained with a 6552-fold purification in a yield of 78% using 2', 5'-ADP Separose 4B affinity gel. Which on SDS polyacrylamide gel electrophoresis showed a single band. Larnoxicam, metronidazole, imipenem, ornidazole, vancomycin, clindamycin, and amoxicillin exhibited inhibitory effects on the enzyme in vitro with IC50 values of 0.17, 0.23, 0.43, 21.79, 46.39, 117.43 and 287.35 mM, and the Ki constants 0.40 +/- 0.04, 0.57 +/- 0.06, 0.77 +/- 0.11, 42.40 +/- 2.89, 65.60 +/- 4.03, 130.22 +/- 9.21, and 287.58 +/- 10.56 mM, respectively. While vancomycin, clindamycin and amoxicillin showed competitive inhibition the other drugs displayed noncompetitive inhibition.     

Inhibition of 6-phosphogluconate dehydrogenase (decarboxylating) by glucose 1,6-bisphosphate.

Glucose 1,6-bisphosphate, the powerful common regulator of several key enzymes in carbohydrate metabolism, was found to exert a potent inhibitory effect on the activity of 6-phosphogluconate dehydrogenase (decarboxylating) from yeast and several rat tissues. These findings suggest that glucose 1,6-bisphosphate may have a regulatory influence on the pentose phosphate pathway.     

Biochemical genetics of Fundulus heteroclitus (L.). III. Inheritance of isocitrate dehydrogenase (Idh-A and Idh-B), 6-phosphogluconate dehydrogenase (6-Pgdh-A), and serum esterase (Est-S) polymorphisms

Starch gel electrophoresis has shown that natural populations of Fundulus heteroclitus have variants at four enzyme-coding loci: Idh-A, Idh-B, 6-Pgdh-A, and Est-S. Analysis of the phenotypic distribution of the F₁ generation suggests that each of the variants segregates as autosomally inherited codominant alleles. Tissue specificity and intracellular localization were also determined for the IDH and 6PGDH isozymes.This work was supported by Grants DEB 76-19877 and DEB 79-12216 from the National Science Foundation and by Grant P60-80-04 from the State of Maryland. RVB and REC were supported by NIH Training Grant GM07231 to the Department of Biology.Contribution No. 1103 from the Department of Biology, The Johns Hopkins University.     

Polymorphism of sorbitol dehydrogenase and 6-phosphogluconate dehydrogenase in swine (Sus scrofa)

More than 300 kidneys from the local bacon factory were investigated and it was shown that the enzyme sorbitol dehydrogenase (EC 1.1.1.14) exhibits a genetically determined polymorphism. While homozygous individuals yield only a single enzyme band after starch gel electrophoresis, heterozygotes show multiple bands.
On the same material also 6-phosphogluconate dehydrogenase (EC 1.1.1.44) and lactate dehydrogenase were investigated, the former showed also clear genetic variants while the latter appeared only in one form.
Gene frequencies for different breeds and types of pigs are given and the results discussed.     

Mercury and the activity of erythrocyte and bone marrow glutathione reductase (E.C. 1.6.4.2.) and glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49) in rats

These studies were carried out on male Wistar rats. Erythrocyte and bone marrow activity of glutathione reductase (GR - E.C. 1.6.4.2) and glucose-6-phosphate dehydrogenase (G6PD - E.C. 1.1.1.49) were determined as affected by mercury. Under physiological conditions the above enzymes were found to be markedly more active in the bone marrow than in erythrocytes. The present experiments have revealed that within the first days there will be an increase in enzyme activity in the bone marrow as well as in glutathione reductase in erythrocytes. Simultaneously, a decline in the activity of erythrocytes could be observed which began within the very first days of the experiments as well as a decrease in the bone marrow, which occurred later in the course of the experiment.     

Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo study

The in vitro and in vivo effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase were investigated. Human erythrocyte 6-phosphogluconate dehydrogenase was purified with ammonium sulphate precipitation, 2',5' ADP-Sepharose 4B affinity and gel filtration chromatography. Some antibiotics (netilmicin sulphate, cefepime, amikacin, isepamycin, chloramphenicol, ceftazidim, teicoplanin, ampicillin, ofloxacin, levofloxacin, cefotaxime, penicillin G, gentamicin sulphate, ciprofloxacin) inhibited enzyme activity in vitro but others (cefozin, decefin, streptomycin, combisid, and meronem) were devoid of inhibitory effects. For the drugs having low IC50 values (netilmicin sulphate and cefepime), in vivo studies were performed in rats. Netilmicin sulphate at 15-mg/kg inhibited enzyme activity significantly (p < 0.001) 1 h, 2 h, and 3 h after dosing and cefepime at 200-mg/kg very significantly (p < 0.001) inhibited the enzyme 1 h and 2 h after dosing. Netilmicin sulphate and cefepime inhibited rat erythrocyte 6-phosphogluconate dehydrogenase both in vivo and in-vitro.     

Effect of mercury, lead and acetylphenylhydrazine (APHZ) on erythrocyte and bone marrow glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49). an electrophoretic study

Male and female rats of Wistar strain have been injected with 0.2% HgCl2, 203HgCl2, PbNO3 and 2% APHZ, in the volume of 0.5 ml saline for 4 days. Subbands of G-6-PD enzyme from erythrocytes and bone marrow cells, were separated by disc polyacrylamide electrophoresis. Four subbands of the enzyme resulted electrophoretic separation. In erythrocytes increase of activity of fraction I. and decrease of fraction II were observed, while in bone marrow opposite reaction was visible. In both tissue following administration of Hg and Pb, fractions III and IV disappeared. In the place of disappeared bands increased radioactivity of 203Hg was detected.