scholarly journals THE QUANTITATIVE HISTOCHEMISTRY OF HYPOTHALAMUS I. PENTOSE SHUNT ENZYMES IN THE ACTIVATED SUPRAOPTIC NUCLEUS OF THE RAT

1967 ◽  
Vol 15 (7) ◽  
pp. 394-398 ◽  
Author(s):  
JOHAN F. JONGKIND
Keyword(s):  
Dehydrogenase Activity ◽  
Supraoptic Nucleus ◽  
Lactic Dehydrogenase ◽  
Glycolytic Enzyme ◽  
Adjacent Area ◽  
Hypothalamic Area ◽  
Quantitative Histochemistry ◽  
Phosphogluconate Dehydrogenase ◽  
Nucleus Supraopticus ◽  
Glucose 6 Phosphate Dehydrogenase

The activities of two enzymes involved in the oxidative part of the pentose cycle and one glycolytic enzyme have been measured by quantitative histochemical methods both in histologically pure nucleus supraopticus and in an adjacent area of the anterior hypothalamus of rat. In the nucleus supraopticus, glucose 6-phosphate dehydrogenase activity increased 34% and 6-phosphogluconate dehydrogenase activity declined by 9%, while lactic dehydrogenase activity did not change significantly after a thirsting period of 6 days. The nonsupraoptic, adjacent anterior hypothalamic area did not show significant changes in activity of any of the enzymes studied.

scholarly journals QUANTITATIVE HISTOCHEMISTRY OF HYPOTHALAMUS II. THIAMINE PYROPHOSPHATASE, NUCLEOSIDE DIPHOSPHATASE AND ACID PHOSPHATASE IN THE ACTIVATED SUPRAOPTIC NUCLEUS OF THE RAT

1969 ◽  
Vol 17 (1) ◽  
pp. 23-29 ◽  
Author(s):  
JOHAN F. JONGKIND
Keyword(s):  
Acid Phosphatase ◽  
Golgi Apparatus ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Supraoptic Nucleus ◽  
Adjacent Area ◽  
Hypothalamic Area ◽  
Quantitative Histochemistry ◽  
Thiamine Pyrophosphatase ◽  
Nucleus Supraopticus

The activities of nucleoside diphosphatases and thiamine pyrophosphatase (TPPase) that are associated with the Golgi apparatus and acid phosphatase were measured by quantitative histochemical methods both in histologically pure nucleus supraopticus and in an adjacent area of the anterior hypothalamus of the rat. In the nucleus supraopticus UDP-phosphohydrolase (UDPase), GDP-phosphohydrolase (GDPase) and TPPase activities increased 40% after a thirsting period of 3 days, while IDP-phosphohydrolase activity increased 18% and acid phosphatase activity decreased 25% after the same osmostic stress. The adjacent, nonsupraoptic anterior hypothalamic area did not show significant changes in activity of any of the enzymes studied. The activities of the Golgi-associated TPPase, UDPase and GDPase are likely to be reliable parameters for neurosecretory activity.

Selective induction and suppression of liver enzyme synthesis

1962 ◽  
Vol 202 (1) ◽  
pp. 137-144 ◽  
Author(s):  
George Weber ◽  
Gouri Banerjee ◽  
Seymour B. Bronstein
Keyword(s):  
Enzyme Activities ◽  
Lactic Dehydrogenase ◽  
Enzyme Synthesis ◽  
Direct Oxidation ◽  
Phosphohexose Isomerase ◽  
Phosphogluconate Dehydrogenase ◽  
Acid Analogue ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Oxidation Of Glucose

Two techniques were used to demonstrate selective induction of enzyme increases in mammalian tissue in vivo: a) refeeding of fasted animals, and b) administration of cortisone to adrenalectomized animals. Refeeding acted selectively as an inducer for the stimulation of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities, and as a less effective inducer of phosphoglucomutase, phosphohexose isomerase, glucose-6-phosphatase, and lactic dehydrogenase. On the other hand, cortisone acted selectively as an inducer for increases in glucose-6-phosphatase, fructose-1, 6-diphosphatase, phosphohexose isomerase and lactic dehydrogenase, and as a less effective inducer of 6-phosphogluconate dehydrogenase. Thus, refeeding primarily stimulated enzymes mediating the direct oxidation of glucose-6-phosphate, whereas cortisone stimulated enzymes involved in gluconeogenesis. The amino acid analogue ethionine selectively inhibited the induced increase of enzyme activities and methionine reversed the ethionine inhibition. The nature of the elevations in the enzyme activities and the mechanisms of ethionine inhibition were discussed.

scholarly journals QUANTITATIVE HISTOCHEMISTRY OF RACHITIC RAT CARTILAGE ENZYME ACTIVITY DURING HEALING INDUCED BY VITAMIN D AND STARVATION

1969 ◽  
Vol 17 (6) ◽  
pp. 411-417 ◽  
Author(s):  
PADMAKAR K. DIXIT
Keyword(s):  
Vitamin D ◽  
Enzyme Activity ◽  
Dehydrogenase Activity ◽  
Lactic Dehydrogenase ◽  
Epiphyseal Cartilage ◽  
Quantitative Histochemistry ◽  
Histochemical Methods ◽  
Cartilage Cells ◽  
Fasted Rats

Quantitative histochemical methods were used for assaying several dehydrogenases in various cell zones of the rachitic rat epiphyseal cartilage during healing brought about by either vitamin D administration or fasting for 48 hr. 6-Phosphogluconic dehydrogenase activity was significantly greater in the cells of both the proliferating and hypertrophic zones of rachitic control rats as compared to those from vitamin D-treated or fasted rats. Activity of 6-phosphogluconic dehydrogenase in the cells from proliferating and hypertrophic zones was identical in the different groups. Lactic dehydrogenase activity of proliferating and hypertrophic cells obtained from rachitic controls was markedly higher than those from the fasted animals. Minor differences were noted in the malic and isocitric dehydrogenases and peptidase in the cartilage cells obtained from vitamin D-treated, untreated and fasted rats.

scholarly journals QUANTITATIVE HISTOCHEMISTRY OF THE NEPHRON. III. LACTIC DEHYDROGENASE ACTIVITY IN MAN AND OTHER SPECIES*

1960 ◽  
Vol 39 (9) ◽  
pp. 1381-1385 ◽  
Author(s):  
Sjoerd L. Bonting ◽  
Victor E. Pollak ◽  
Robert C. Muehrcke ◽  
Robert M. Kark
Keyword(s):  
Dehydrogenase Activity ◽  
Lactic Dehydrogenase ◽  
Quantitative Histochemistry

Maleimide as an inhibitor in measurement of erythrocyte glucose-6-phosphate dehydrogenase activity.

1978 ◽  
Vol 24 (6) ◽  
pp. 885-889 ◽  
Author(s):  
J Deutsch
Keyword(s):  
Dehydrogenase Activity ◽  
Coefficient Of Variation ◽  
Present Method ◽  
Reaction Rate ◽  
Hemoglobin Concentration ◽  
Statistical Correlation ◽  
Secondary Reaction ◽  
Phosphogluconate Dehydrogenase ◽  
Reagent Cost ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract Erythrocyte glucose-6-phosphate dehydrogenase activity is measured with a centrifugal analyzer by use of a commercial reagent kit and of the reaction glucose-6-phosphate + NADP+ leads to 6-phosphogluconolactone + NADPH. Rate of production of NADPH is measured and related to hemoglobin concentration. Maleimide is added to inhibit further production of NADPH in a secondary reaction by endogenous 6-phosphogluconate dehydrogenase. The method is compared with others that are designed to circumvent the secondary reaction by either (a) addition of excess phosphogluconate dehydrogenase to drive the secondary reaction to completion or (b) inhibition of endogenous phosphogluconate dehydrogenase by 2,3-diphosphoglycerate. The present method has the advantages that reaction rate more quickly becomes linear and reagent cost is less as compared with other methods. The within-run coefficient of variation was 3%. The various methods investigated showed good statistical correlation.

Measurement of Glucose-6-phosphate Dehydrogenase and 6-Phosphogluconate Dehydrogenase Activites in Erythrocytes by Use of a Centrifugal Analyzer

1974 ◽  
Vol 20 (10) ◽  
pp. 1349-1352 ◽  
Author(s):  
John F Nicholson ◽  
Selma H Bodourian ◽  
Michael A Pesce
Keyword(s):  
Dehydrogenase Activity ◽  
Dehydrogenase Deficiency ◽  
Simple Modification ◽  
Phosphogluconate Dehydrogenase ◽  
Automated Method ◽  
Large Populations ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract We describe an accurate automated method for measuring activity of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) in erythrocytes with a centrifugal analyzer. Blood is collected in microhematocrit tubes, centrifuged, and the erythrocytes are lysed with digitonin. Glucose-6-phosphate dehydrogenase activity is determined by mixing the hemolysate with glucose-6-phosphate, NADP+, and 6-phosphogluconate dehydrogenase #{ 233} (EC 1.1.1.44) in triethanolamine—EDTA buffer at pH 7.6, and measuring the rate of NADPH production for 3 min. Under these conditions 2 mol of NADPH are produced per mole of glucose-6-phosphate oxidized, ensuring the accuracy of the method and increasing its sensitivity. Activity is referred to hemoglobin, measured as cyanmethemoglobin. Activity of glucose-6-phosphate dehydrogenase added to hemolysates was well accounted for. Results obtained by our method and by the method of Bishop [J. Lab. Clin. Med. 68, 149 (1966)] are virtually identical. Our method requires a small amount of blood and is accurate and rapid; thus it is well suited for use in surveying large populations for glucose-6-phosphate dehydrogenase deficiency. A simple modification of the method may be used to determine the activity of 6-phosphogluconate dehydrogenase.

scholarly journals Stimulation of pentose phosphate pathway dehydrogenase enzyme activities in ethionine-treated mice

1968 ◽  
Vol 106 (4) ◽  
pp. 769-776 ◽  
Author(s):  
Hsien-Gieh Sie ◽  
William H. Fishman
Keyword(s):  
Dehydrogenase Activity ◽  
Fold Increase ◽  
Pentose Phosphate ◽  
Hepatic Glycogen ◽  
Synthetase Activity ◽  
Phosphogluconate Dehydrogenase ◽  
Glycogen Synthetase ◽  
Period 2 ◽  
Marked Preference ◽  
Glucose 6 Phosphate Dehydrogenase

1. Mice treated with ethionine (intraperitoneally, 5mg./day for 4 days or 10mg./day for 3 days) showed a profound loss of hepatic glycogen, a decrease of glycogen synthetase activity, a development of hypoglycaemia, a two- to five-fold increase in the activity of glucose 6-phosphate dehydrogenase but no change in 6-phosphogluconate dehydrogenase and an earlier manifestation of the solubilization of phosphorylase as compared with glycogen synthetase. The administration of ATP did not prevent these effects. 2. During the early post-injection period (2–3 days) there was a further enhancement of the activity of glucose 6-phosphate dehydrogenase (tenfold) in the liver and a clear elevation of 6-phosphogluconate dehydrogenase activity (twofold). Subsequently, the glycogen concentration was restored, followed by an earlier reassociation of glycogen particle with phosphorylase than with glycogen synthetase, along with a disappearance of ethionine effect at about the eighteenth day. 3. Glucose 6-phosphate dehydrogenase from both control and ethionine-treated animals showed a marked preference for glucose 6-phosphate as substrate rather than for galactose 6-phosphate, whose rate of oxidation was only 10% of that of the glucose 6-phosphate. 4. Since actinomycin D, puromycin, 5-fluorouracil and dl-p-fluorophenylalanine failed to block the ethionine-enhanced glucose 6-phosphate dehydrogenase activity, the possibility that new enzyme protein synthesis is responsible for the effect is doubtful.

6-Phosphogluconate Dehydrogenase, Glucose-6-Phosphate Dehydrogenase, Glucose-6-Phosphate Isomerase, and Hexokinase Activity Ratios in Some Human Tumor Cytosols

1978 ◽  
Vol 64 (6) ◽  
pp. 579-586
Author(s):  
Michele Miranda ◽  
Terenzio Ventura ◽  
Luciano Iorio ◽  
Anna M. Ragnelli ◽  
Claudio Martano ◽  
...  
Keyword(s):  
Cell Growth ◽  
Dehydrogenase Activity ◽  
Human Tumor ◽  
Hexokinase Activity ◽  
Phosphogluconate Dehydrogenase ◽  
Growth Requirements ◽  
High K ◽  
Activity Ratios ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Low K

The ratios of some key enzymatic activities of carbohydrate metabolism have been measured in human tumor cytosols. The activities of whole hexokinase (low Km, EC 2.7.1.1 and high Km, EC 2.7.1.2), 6-phosphogluconate dehydrogenase (EC 1.1.1.43), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and glucose-6-phosphate isomerase (EC 5.3.1.9) change according to a biochemical pattern coherent with cell growth requirements. 6-phosphogluconate dehydrogenase activity was in each sample tested higher than glucose-6-phosphate dehydrogenase activity; this indicates that 6-phosphogluconate, a powerful inhibitor of glucose-6-phosphate isomerase, is unlikely to accumulate and inhibit this enzyme and glucose-6-phosphate channelling into glycolysis.

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