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At least 19 recordsLinked to original sources
PubMed1979

Partial purification, substrate specificity and regulation of alpha-L-glycerolphosphate dehydrogenase from Saccharomyces carlsbergensis.

alpha-L-Glycerolphosphate dehydrogenase (sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase, EC 1.1.1.8) from Saccharomyces carlsbergensis was purified 400-fold. The enzyme preparation is free of interfering activities, such as glyceraldehyde phosphate dehydrogenase, alcohol dehydrogenase, triose phosphate isomerase and glycerolphosphatase. At pH 7.0 it is specific for NADH (Km = 0.027 mM with 0.8 mM dihydroxyacetone phosphate) and dihydroxyacetone phosphate (Km = 0.2 mM with 0.2 mM NADH). Between pH 5.0 and 6.0 the enzyme functions with NADPH, but only at 7% of the rate with NADH. Various anions (I- greater than SO42- greater than Br- greater than Cl-) act as inhibitors competing with the substrate dihydroxyacetone phosphate. Inorganic phosphate (Ki = 0.1 mM), pyrophosphate and arsenate are strong inhibitors. The nucleotides ATP and ADP are also inhibitory, but their action seems to be of the same type as the general anion competition (Ki = 0.73 mM for ATP). The results are consistent with the notion that the enzyme may regulate the redox potential of the NAD+/NADH couple during fermentation.

Adenine Nucleotides↗
PubMed1979

[Nonspecific esterase and alpha-glycerolphosphate dehydrogenase activity and the fat content in the regenerating chicken liver].

The data on histochemical study of changes in the activity of esterases, alpha-glycerophosphate dehydrogenase and the fat content in the chick regenerating liver are presented. The accumulation of the fat in hepatocytes during the early periods of regeneration (1--5th day of the experiment) is partially conditioned by the reduction of the activity of nonspecific esterases. The maximal liver steatosis is accompanied also by an increase in the activity of alpha-glycerophosphate dehydrogenase which indicates intensification of glycolysis and synthesis of triacylglycerines (liver spare lipids) during regeneration.

Animals↗
PubMedDate not supplied

[alpha-glycerolphosphate dehydrogenase activity in rabbit organs and tissues in various endocrine disorders].

Activity of alpha-glycerophosphate dehydrogenase (GPDG) from rabbit tissues was distinctly decreased in hypothyroidism and increased in hyperthyroidism. In alloxane diabetes and after administration of high doses of insulin the GPDG activity, and especially the activity of its mitochondrial form, was markedly decreased in kidney and heart tissues; it was unaltered or slightly increased in liver tissue and sceletal muscles, as compared with control. The hormonal regulation of the GPDG activity is a complicated process, in which are involved not only the hormones of thyroid gland but also hormones of other endocrine glands.

11-Hydroxycorticosteroids↗
PubMed1979

Influence of androgens on the weights of the male accessory reproductive organs and on the activities of mitochondrial enzymes in the epididymis of the rat.

The influence of androgens on the male accessory glands of the rat was assessed in terms of changes in weight and of the specific activity of the mitochondrial enzymes, succinate dehydrogenase, glycerolphosphate dehydrogenase and pyruvate carboxylase, in the epididymis. In some instances, the activity of the cytoplasmic enzymes, hexokinase and phosphofructokinase, was also measured and the influence of androgens on these enzymes was found to be similar to that on the mitochondrial enzymes. After the administration of androgen to castrated rats the specific activity of enzymes reached a new steady state sooner than did epididymal weight. The time taken for the specific activity of the enzymes to reach a new steady state after the removal of androgen was variable, depending on the enzyme and the region of the epididymis. This time was generally longer, however, than the time taken for induction, and in the case of glycerolphosphate dehydrogenase, the decline of activity was slower in the cauda than in the caput. In castrated animals, about 100 times as much androgen was required to attain maximum tissue weight as was required to attain maximum enzyme activity. The epididymis, prostate and seminal vesicles responded similarly to androgen in terms of the dose-response pattern and the time taken for tissue weight to attain a new steady-state value, although the gain in weight of the epididymis relative to its weight in unstimulated control animals was less than the relative gain of the other accessory glands. Enzymes in the cauda epididymidis required lower amounts of androgen to elicit maximum activity than were required by those in the caput. The rate of change in the accessory glands in attaining new steady-state levels of tissue weight and enzyme activity was independent of the dose of androgen except during the first few days of hormone administration. Androgens were the most effective steroids in stimulating an increase of tissue weight and enzyme activity, although some changes were induced by oestradiol-3-benzoate and progesterone.

Animals↗
PubMed1979

Effects of ischaemia on enzyme-activities in the soleus muscle of the rat.

1. The changes with the time of the activities of some energy-supplying enzymes and of the hydrolytic enzyme, acid phosphatase, were studied over 2 weeks of complete ischaemia, produced in the rat soleus muscle by section of the abdominal aorta and terminal devascularization, leaving nerve and tendon intact. 2. Activities of glycolytic enzymes, oxidative enzymes, hexokinase and acid phosphatase are affected in a different manner. Activities of the glycolytic enzymes, lactate dehydrogenase, triosephosphate dehydrogenase and glycerolphosphate dehydrogenase, are lowest on the 1st day and increase thereafter. The first two reach the control values again on the 4th and 14th day, respectively, while glycerolphosphate dehydrogenase reaches about 50% of the control value on the 14th day. The maximum decrease in activity of the oxidative enzymes, citrate synthase, beta-hydroxyacyl-CoA-dehydrogenase and malate dehydrogenase occurs later (4th day); thereafter their activity returns slowly to control values, but does not reach them even on the 14th day. Hexokinase activity is slightly decreased on the 1st day; then it increased and reached on the 7th day twice the control value. Thus on the 1st day the activity of the enzymes of aerobic metabolism prevail, and on the 4th day those of anaerobic carbohydrate (glucose) metabolism; the recovery of enzyme activity of aerobic oxidation occurs later. 3. Acid phosphatase activity increased from the 2nd day onwards, reaching up to 3 times the control value on the 4th day and still twice that value on the 14th day. This agrees well with the histochemical picture of acid phosphatase. 4. Histochemical changes of alkaline phosphatase activity reveal destruction of capillary endothelial cells during the first few days after operation and their later proliferation from the periphery, correlating with the loss and recovery of oxidative enzyme activity.

3-Hydroxyacyl CoA Dehydrogenases↗
PubMed1975

Histochemistry of trauma after electrode implantation and stimulation in the hippocampus.

Electrodes were implanted into the rat hippocampus in both hemispheres for increasing periods of up to 60 days, and the effects of trauma and electrical stimulation of enzymes controlling cell metabolism in the region of implantation were examined and assessed in relation to studies on humans. In the unstimulated hippocampus as a control, enzyme changes were mainly confined to a narrow area of tissue damage surrounding the electrode. The enzyme changes in response to trauma varied widely; some enzymes controlling tissue respiration showed early and rapid changes, increasing in hyperactive, swollen glial cells and vascular endothelium and decreasing in nerve cells and neuropile. Acid phosphatase activity also increased rapidly in glial cells; other phosphate-releasing enzymes increased more gradually with time. A turning point in these chages was apparent between 25 and 40 days, followed by a reversion to more normal levels at 60 days. Electrical stimulation of the hippocampus in the contralateral hemisphere produced no detectable enzyme changes from those of the unstimulated hippocampus.

Acetylcholinesterase↗
PubMed1979

Postnatal development of peroxisomal and mitochondrial enzymes in rat liver.

Subcellular organellles from livers of rats three days prenatal to 50 weeks postnatal were separated on sucrose gradients. The peroxisomes had a constant density of 1.243 g/ml throughout the life of the animal. The density of the mitochondria changed from about 1.236 g/ml at birth to a constant value of 1.200 g/ml after two weeks. The peroxisomal and mitochondrial fatty acid beta-oxidation and the peroxisomal and supernatant activities of catalase and glycerol-3-phosphate dehydrogenase were measured at each age, as well as the peroxisomal core enzyme, urate oxidase, and the mitochondrial matrix enzyme, glutamate dehydrogenase. All of these activities were very low or undetectable before birth. Mitochondrial glutamate dehydrogenase and peroxisomal urate oxidase reached maximal activities per g of liver at two and five weeks of age, respectively. Fatty acid beta-oxidation in both peroxisomes and mitochondria and peroxisomal glycerol-3-phosphate dehydrogenase exhibited maximum activities per g of liver between one and two weeks of age before weaning and then decreased to steady state levels in the adult. Peroxisomal beta-oxidation accounted for at least 10% of the total beta-oxidation activity in the young rat liver, but became 30% of the total in the liver of the adult female and 20% in the adult male due to a decrease in mitochondrial beta-oxidation after two weeks of age. The greatest change in beta-oxidation was in the mitochondrial fraction rather than in the peroxisomes. At two weeks of age, four times as much beta-oxidation activity was in the mitochondria as in the peroxisomal fraction. Peroxisomal glycerol-3-phosphate dehydrogenase activity accounted for 5% to 7% of the total activity in animals younger than one week, but only 1% to 2% in animals older than one week. Up to three weeks of age, 85% to 90% of the liver catalase was recovered in the peroxisomes. The activity of peroxisomal catalase per g of rat liver remained constant after three weeks of age, but the total activity of catalase further increased 2.5- to 3-fold, and all of the increased activity was in the supernatant fraction.

Age Factors↗
PubMed1975

Histochemical properties of skeletal muscle fibers in streptozotocin-diabetic rats.

The response of rat gastrocnemius muscle fibers to chronic streptozotocindiabetes was studied. Transverse sections of this muscle from normal and diabetic rats were histochemically assayed for reduced diphosphopyridine nucleotide-diaphorase, myofibrillar adenosine triphosphatase, mitochondrial alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, and alkaline phosphatase activities. Cross-sectional areas of the fiber types were measured, and fiber capillarization and populations estimated. Chemically-induced diabetes appeared to have little effect on the metabolic or morphological properties of slow-twitch fibers. However, a general dedifferentiation occurred in the 2 fast-twitch fiber populations. There was a loss of oxidative potential in the fast-twitch-oxidative-glycolytic fibers, and a significant decrease in size in the fast-twitch-glycolytic fibers. No change in the proportions of slow- and fast-twitch fibers in the muscles of diabetic rats occurred. It is concluded that hypoinsulinism has differential effects on the 3 fiber types in heterogeneous rat skeletal muscle, and that slow-twitch fibers are least affected by the diabetic condition.

Adenosine Triphosphatases↗
PubMed1975

[Representative enzymes of energy supplying metabolism in the normal and denervated human brachial biceps, deltoid and anterior tibial muscles (author's transl)].

Representative enzyme activities of energy supplying metabolism were measured in muscle specimens of brachial biceps, deltoid or anterior tibial muscle of patients with affections of the peripheral nerves. Simultaneously performed measurements of the same enzyme activities in the contralateral normal muscles served as a control. 5 patients suffered from a lesion of the brachial plexus, 7 patients had a paralysis of the axillary nerve, and 8 patients had a peroneal paralysis. In all denervated muscles no electrophysiological signs of reinnervation were present. The activities of glycogen phosphorylase, triosephosphate dehydrogenase, lactate dehydrogenase and alpha-glycerophosphate dehydrogenase were found to be highest in the normal brachial biceps muscle. Lower activities were measured in the normal deltoid and anterior tibial muscle. The oxidative enzymes, 3-hydroxyacyl-CoA dehydrogenase and citrate synthase as well as hexokinase, showed no significant difference from the levels of the control. It is suggested that a probable factor determining the differences of the enzyme activities of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation between brachial biceps, deltoid and anterior tibial muscle, might be the pattern of impulse activity in the motor nerves of these muscles. The enzyme activities of glycogen phosphorylase, triosephosphate dehydrogenase, lactate dehydrogenase and alpha-glycerophosphate dehydrogenase, decreased rapidly during the first 2 months after denervation in the brachial biceps, deltoid and anterior tibial muscle, whereas the decrease was slight during the following months. The activities of the oxidative enzymes (3-hydroxyacyl-CoA dehydrogenase and citrate synthase) showed no significant change after denervation. The metabolic difference of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation between the three muscles was no longer maintained. The possible causes of the deeply decreased enzyme activities of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation, as well as the causes of the unchanged oxidative enzyme activities and of the increased hexokinase activity after denervation in the human brachial biceps, deltoid and anterior tibial muscle, are discussed.

Adolescent↗
PubMed1976

Electrophoretic variability in island populations of Drosophila simulans and Drosophila immigrans.

Genetic structure and variability were investigated in several Hawaiian populations of D. simulans and D. immigrans. Genetic variability is lower in Hawaiian populations of D. simulans than in Texas populations, and allelic differences exist as well. For D. immigrans, Hawaiian and Korean populations are similar in variability, allelic content, and gene frequencies. Several hypothesis are advanced to account for the patterns in gene variation observed between island and continental populations of these two colonizing species.

Alcohol Oxidoreductases↗
PubMed1978

Enzyme histochemical studies on the Purkinje fibers of the atrioventricular system of the bovine and porcine hearts.

In this communication the results of applying various histochemical semipermeable membrane techniques to the localization of several enzymes in bovine and porcine heart are presented. The Purkinje fibers of the atrioventricular conducting system of the bovine heart differ from the myocardium proper in containing a greater activity of the glycolytic and gluconeogenetic enzymes--lactate dehydrogenase, glyceraldehyde-phosphate dehydrogenase, hexokinase, glucosephosphate isomerase and phosphoglucomutase, and less activity of the aerobic enzymes--NADH: nitroBT oxidoreductase and isocitrate dehydrogenase (NADP+). The metabolic reactions obtained with Purkinje fibers of the porcine heart are less pronounced. These histochemical findings are in accordance with the impression that Purkinje fibers, compared with the common myocardial fibers, have a higher rate of anaerobic metabolism and a lower rate of aerobic metabolism. The activity of the NADPH regenerating enzymes glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating), and the activity of acid hydrolases such as non-specific esterase and acid phosphatase is higher in the Purkinje fibers of both the bovine and porcine heart.

Animals↗
PubMed1976

Morphometric and enzyme histochemical behaviour of the kidney of young rats before and after unilateral nephrectomy.

Four week old male Wistar rats were unilaterally nephrectomized, and one, two, four, fourteen, and twenty-eight days after the operation the remaining kidneys were removed for morphological examination--including measurement of diameters of the tubules--and for histochemical investigation of enzymatic activities in the nephrons. The following enzymes were examined: succinate DH, lactate DH, alpha-glycerophosphate DH, isocitrate DH, glucose-6-phosphate DH, cytochrome oxidase, adenosine triphosphatase, alkaline and acid phosphatases. In comparison with kidneys of control animals of the same age and sex, the hypertrophy of the remaining kidney was found to be, even in these young rats, entirely due to enlargement of preexisting nephrons. The measurements have indicated that the hypertrophy was most distinct between the second and fourth day after uninephrectomy. Four weeks after the operation the diameters of proximal and distal tubules were about 21% and 18% respectively bigger in the uninephrectomized animals than in the corresponding controls. This increase in size was accompanied by some changes in intensity of enzymatic staining reactions; after an initial diminishment, a graduate increase in activity of almost all the observed tubular enzymes was found; this seems to be the expression of the functional compensation by the remaining kidney.

Adaptation, Physiological↗
PubMed1976

Cholesterol and fatty acid synthesis in swine.

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.

ATP Citrate (pro-S)-Lyase↗
PubMed1977

Effects of progesterone on some enzymes of fat and carbohydrate metabolism in rat liver.

The known effect of progesterone on carbohydrate metabolism prompted a study of some of the hepatic "lipogenic" and "gluconeogenic" enzymes in rats treated with progesterone. Several enzymes providing lipid precursors (phosphofructokinase, malic enzyme, glucose-6-phosphate dehydrogenase, and citrate cleavage enzyme) showed increased specific activity. These changes may represent insulin effects. Specific activity of phosphoenolpyruvate carboxykinase, usually associated with control of gluconeogenesis, was also increased. The latter is compatible with increased capability for glycogenesis, which is recognized as a progesterone effect.

ATP Citrate (pro-S)-Lyase↗