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Query: EC:1.1.1.49 (
glucose-6-phosphate dehydrogenase
)
7,794
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Testicular tissue was shown to contain the full complement of enzymes required for de novo synthesis of fatty acids. The enzymes capable of snythesizing palmitic acid from citrate, acetate, or acetyl CoA were found to be present in the soluble (cytoplasmic) fraction. These included fatty acid synthetase, acetyl CoA carboxylase, citrate-cleavage enzyme, malic enzyme,
glucose-6-phosphate dehydrogenase
, and
6-phosphogluconate dehydrogenase
. Optimal conditions for assaying activities of fatty acid synthetase and acetyl CoA carboxylase in the soluble fraction from rat testes were established, and the activities of these two enzymes were determined to be 0.54 +/- 0.1 and 0.030 +/- 0.002 (nmoles of substrate incorporated into fatty acid per min per mg of soluble fraction protein), respectively. The activities of citrate-cleavage enzyme, malic enzyme, and the
glucose-6-phosphate dehydrogenase
/
6-phosphogluconate dehydrogenase
pair were also measured. The activities were 6.0 +/- 0.7, 34.9 +/- 4.2, and 29.9 +/- 9.3 nmoles/min/mg, respectively.
...
PMID:Studies in vitro of lipogenesis in rat testicular tissue. 0 21
Highly purified platelet
glucose-6-phosphate dehydrogenase
(G6PD;
D-glucose-6-phosphate:NADP+ 1-oxidoreductase
,
EC 1.1.1.49
) can be modified in its isoelectric point and its molecular specific activity by extracts of some leukemic granulocytes. The "G6PD modifying factors" are relatively small molecules (molecular weight slightly under 5000), thermostable, dialyzable, and ultrafilterable. These molecules are destroyed by various endo- and exopeptidases and by serine enzymes present in crude extracts of leukocytes and commercial preparations of ribonuclease. The alterations of platelet G6PD due to the "G6PD modifying factors" are stable and not reversible by dialysis or further chromatography. The leukemic extracts which are able to modify G6PD also can modify the electrophoretic mobility and (or) the enzymatic activity of purified leukocyte pyruvate kinase,
6-phosphogluconate dehydrogenase
, and glucosephosphate isomerase. The chemical nature of such modifications and their relationships with post-translational modifications which occur in leukemic or normal cells are discussed.
...
PMID:Modifications of purified glucose-6-phosphate dehydrogenase and other enzymes by a factor of low molecular weight abundant in some leukemic cells. 0 52
Several mammary and adipose enzymes were measured in normal, adrenal-ectomized, adrenalectomized cortisol-treated, and intake-restricted lactating rats. Acetyl-CoA carboxylase, lipoprotein lipase, and triglyceride synthetase complex activities in mammary tissue were unchanged by intake restriction, decreased by adrenalectomy, and increased by glucocorticoid-replacement therapy. Malic dehydrogenase,
glucose-6-phosphate dehydrogenase
,
6-phosphogluconate dehydrogenase
, and lipoprotein lipase activities in adipose were unchanged after adrenalectomy.
...
PMID:Effects of adrenalectomy and glucocorticoid therapy on enzyme activities in mammary and adipose tissues from lactating rats. 0 27
In incubation studies with swine tissue slices, acetate-1-14C or glucose-U-14C as substrates were incorporated more readily into fatty acids and cholesterol in adipose tissue than other tissues tested. Cholesterol and fatty acid synthesizing acitivity was substantial in the small intestine. When acetate was available, liver, small intestine, and adipose tissue were important sites for cholesterol synthesis. Heart and aortic tissue had marginal levels of cholesterol synthesizing ability. Lipogenesis in adult swine liver, heart, and aortic tissue was extremely low. As in tissue slices, incorporation of acetyl-1-14C CoA into fatty acids by adipose homogenates indicated high lipogenic activity. Subcellular fractionations of heart and aortic tissue indicated that the heart microsomal fraction had the highest lipogenic activity as measured by the incroporation of acetyl-4-14C CoA into fatty acids. In adult swine adipose tissue, the incorporation of glucose-U-14C into fatty acid was higher than its incorporation into glyceride-glycerol. The synthesis of glyceride-glycerol from glucose-U-14C or acetate-1-14C in liver was higher than for fatty acid synthesis. The acitivity of acetyl CoA carboxylase, fatty acid synthetase, citrate cleavage enzyme, nicotinamide adenine dinucleotide phosphat-malate dehydrogenase,
glucose-6-phosphate dehydrogenase
, and
6-phosphogluconate dehydrogenase
was considerably higher in adipose tissue than in other tissues tested, paralleling its high lipogenic capacity.
...
PMID:Cholesterol and fatty acid synthesis in swine. 0 32
The levels of the adenine nucleotides, pyridine nucleotides and the kinetical parameters of the enzymes of the Entner-Doudoroff pathway (
glucose-6-phosphate dehydrogenase
and
6-phosphogluconate dehydrogenase
) were determined in Azotobacter vinelandii cells, grown under O2- or N2-limiting conditions. It was concluced that the levels of both the adenine nucleotides and pyridine nucleotides do not limit the rate of sucrose oxidation. Experiments with radioactive pyruvate and sucrose show that the rate of sucrose oxidation of Azotobacter cells is associated with an increase in the rate of sucrose uptake. The sites of oxidative phosphorylation and the composition of the respiratory membranes with respect to cytochromes c4 + c5, b and d differ in cells growth either O2- or N2-limited. It was possible to show that the respiration protection of the nitrogen-fixing system in Azotobacter is mainly independent of the oxidation capacity of the cells. The oxidation capacity intrinsically depends on the type of substrate and can be partly adapted. The maximum activity of the nitrogenase in Azotobacter depends on the type of substrate oxidized. Although the level of energy charge is somewhat dependent on the type of substrate used, no obvious relation can be derived between changes in energy charge and nitrogenase activity. An alternative proposal is given.
...
PMID:Regulation of respiration and nitrogen fixation in different types of Azotobacter vinelandii. 0 24
Feeding sheep a concentrate diet compared with grass diets increased the hepatic specific activities of the three glycolytic enzymes studied, and that of
glucose-6-phosphate dehydrogenase
(
EC 1.1.1.49
) and reduced the specific activity of D-fructose-I, 6-diphosphate I-phosphohydrolase (EC 3.1.3.11). The specific activities of
phosphogluconate dehydrogenase
(EC 1.1.1.43) and malate dehydrogenase (decarboxylating) (NADP) (EC 1.1.1.40) were unaffected by diet.
...
PMID:The effects of grass and concentrate diets on the specific activities of some enzymes of hepatic carbohydrate metabolism in sheep. 0 5
The analogue of fructose 1,6-bisphosphate in which the phosphate group, -O-PO3H2, on C-6 is replaced by the phosphonomethyl group, -CH2-PO3H2, was made enzymically from the corresponding analogue of 3-phosphoglycerate. It was a substrate for aldolase, which was used to form it, but not for fructose 1,6-bisphosphatase. It was hydrolysed chemically to yield the corresponding analogue of fructose 6-phosphate [i.e. 6-deoxy-6-(phosphonomethyl)-D-fructose, or, more strictly, 6,7-dideoxy-7-phosphono-D-arabino-2-heptulose]. This proved to be a substrate for the sequential actions of glucose 6-phosphate isomerase,
glucose-6-phosphate dehydrogenase
and
6-phosphogluconate dehydrogenase
. Thus seven out of the nine enzymes of the glycolytic and pentose phosphate pathways so far tested catalyse the reactions of the phosphonomethyl isosteres of their substrates.
...
PMID:Phosphonomethyl analogues of hexose phosphates. 0 47
The development of obesity, hyperinsulinemia and six hepatic lipogenic enzymes in Avy/a mice were compared to that in a/a mice. Correlation between body weight, liver weight, plasma insulin concentration and activities of hepatic enzymes was analyzed. In the Avy/a mice, body weight, liver weight and plasma insulin level increased steadily as the mice aged. In the a/a mice, the change of these three parameters was much slower. Plasma insulin concentration in a/a mice did not increase until eight months of age. Compared with a/a mice, Avy/a mice had higher
6-phosphogluconate dehydrogenase
and fatty acid synthetase activities at two months of age; lower citrate cleavage enzyme,
glucose-6-phosphate dehydrogenase
and
6-phosphogluconate dehydrogenase
activities at three months of age; lower citrate cleavage enzyme and
glucose-6-phosphate dehydrogenase
and higher acetyl CoA carboxylase activities at five months of age; and higher malic enzyme, citrate cleavage enzyme and
6-phosphogluconate dehydrogenase
activities at eight months of age. There were significant correlations between plasma insulin level and body weight and between plasma insulin level and the activities of malic enzyme and citrate cleavage enzyme in Avy/a mice. The correlation between body weight and malic enzyme and citrate cleavage enzyme activities disappeared after the analysis was adjusted for plasma insulin level.
...
PMID:An analysis of the relationships among obesity, plasma insulin and hepatic lipogenic enzymes in "viable yellow obese" mice (Avy/a). 0 20
Fatty acid synthesis was studied in testes of rats fed a fat-free or fat-supplemented diet. Testes of fat-deficient rats incorporated nearly twice as much intratesticularly injected [1-14C]acetate into total fatty acids (primarily into palmitic acid) as did supplemented rats. To determine the mechanism for the increased synthesis, the activities of the following enzymes were determined in the cytoplasmic fraction of testicular homogenates: fatty acid synthetase, acetyl CoA carboxylase [EC 6.4.1.2], citrate-cleavage [EC 4.1.3.8], malic [EC 1.1.1.38], and the glucose-l-phosphate dehydrogenase [
EC 1.1.1.49
]:
6-phosphogluconate dehydrogenase
pair [EC 1.1.1.44]. Although the activity of fatty acid synthetase did increase in livers from fat-deficient rats, no change was observed in corresponding testes. No difference between the two groups could be demonstrated in testicular activity of citrate-cleavage enzyme, malic enzyme, or the
glucose-6-phosphate dehydrogenase
:
6-phosphogluconate dehydrogenase
pair. However, the activity of cytoplasmic acetyl CoA carboxylase in testes of rats fed the fat-deficient diet was 1.4 times higher than the activity in testes of rats fed the supplemented diet. Fat deficiency did not affect the specific activity of the testicular microsomal elongation system, assayed by incubation with 14C-malonyl CoA. The concentration of unesterified fatty acids was lower in testes of the fat-deficient compared to supplemented rats, indicating that decreased inhibition of acetyl CoA carboxylase in the fat-deficient rats testes might have been responsible for the observed increased de novo synthesis of palmitic acid.
...
PMID:Fatty acid synthesis in testes of fat-deficient and fat-supplemented rats. 1 68
1.
6-phosphogluconate dehydrogenase
from sheep liver has been purified 350-fold by affinity chromatography with a final specific activity of 18 micronmol of NADP+/reduced min per mg of protein and an overall yield of greater than 40%. 2. A systematic investigation of potential ligands has been carried out: these included 6-phosphogluconate and NADP+, pyridoxal phosphate and several immobilized nucleotides. The results indicate that NADP+ is the most suitable ligand for the purification of
6-phosphogluconate dehydrogenase
. 3. The effects of pH and alternative eluents have been examined in relation to the parameters known to affect the desorption phase of affinity chromatography; careful manipulation of the elution conditions permitted the separation of
glucose 6-phosphate dehydrogenase
, glutathione reductase and
6-phosphogluconate dehydrogenase
from sheep liver on NADP+-Sepharose 4B. 4. A large-scale purification scheme for
6-phosphogluconate dehydrogenase
is presented that uses the competitive inhibitors inorganic pyrophosphate and citrate as specific eluents.
...
PMID:An examination of potential matrices for the affinity chromatography of NADP+-linked dehydrogenases with special reference to 6-phosphogluconate dehydrogenase. 1 50
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