Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of aspartate transminase (EC 2.6.1.1), alanine transminase (EC 2.6.1.2), alkaline phosphatase (EC 3.1.3.1), acid phosphatase (EC 3.1.3.2) leucine arylamidase (EC 3.4.1.1), aldolase (EC 4.1.2), lactate dehydrogenase (EC 1.1.1.27), malate dehydrogenase (EC 1.1.1.38) and cholinesterase (EC 3.1.1.7) were measured in serum of male rabbits and albino Wistar rats in dlplicate by means of microliter techniques. Furthermore, the diurnal alterations of enzyme activity were established in 8--10 animals of both species. Aspartate transaminase activity in the serum of rats was found to be significantly higher than in the serum of humans and rabbits, and essentially lower alkaline phosphatase values were obtained from the serum of rabbits in comparison with those found for the serum of humans and rats. Relatively high acid phosphatase and aldolase values as well as a very low cholinesterase activity were found in the serum of rabbits and rats. The mean malate dehydrogenase-activity was found to be twice as high as the mean lactate dehydrogenase, which is the contrary of the situation found in human serum. No significant diural alterations of the examined enzyme activities were established. The differences found between the animal and the human enzyme activities in serum are explained by species-determined peculiarities of metabolism or specific enzyme configuration.
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PMID:[Enzyme activities in serum of rabbits and rats-reference values and circadian alterations. Serum enzymes and factors that influence their activity,I (AUTHOR'S TRANSL)]. 103 68

Histologic investigations together with histochemical and photometric measurements of enzyme activities were performed in retina of rabbits, whose blood supply had been totally interrupted for 1h. A retinal edema developed affecting the internal layers between the inner limiting membrane and the internal plexiform and ganglion cell layer. Although this edema was quite remarkable at the posterior pole of the eye, it diminished toward the periphery, disappearing near the ora serrata. The activities of the following enzymes were investigated: hexokinase, glucose 6-phosphate dehydrogenase, aldolase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, succinate dehydrogenase, ATPase, and phosphorylase. The most striking finding was the total disappearance of phosphorylase activity under pressure ischemia. ATPase and aldolase showed a decreased activity in the ischemic retina, and malate dehydrogenase a slightly diminished one. Concerning the other enzymes, no significant differences between normal and ischemic retina were observed.
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PMID:Enzymologic and histologic investigations in normal and pressure-ischemic retina of rabbits. 108 79

1. The effects of protein concentration and ionic strength on the adsorption of the individual glycolytic enzymes to F-actin and F-actin--trypomyosin--troponin have been studied. 2. Appreciable association was demonstrated under conditions of physiological ionic strength and high protein concentration, and tropomyosin--troponin established as an important and generalized component of these interactions. 3. Phosphofructokinase, aldolase, pyruvate kinase, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and glucose-6-phosphate isomerase were strongly bound under these conditions, while triosephosphate isomerase, phosphoglycerate kinase, phosphoglycerate mutase, enolase and hexokinase displayed less adsorption to the structural proteins. 4. The influence of a number of parameters on the adsorption phenomena was examined. Ca2+ and fructose 1,6-diphosphate increased the adsorption of aldolase, lactate dehydrogenase and pyruvate kinase, while decreasing the adsorption of the enzymes of the constant-proportion group. 5. Of the other major enzymic components of skeletal muscle, creatine kinase, adenylate kinase and malate dehydrogenase showed no adsorption to F-actin--tropomyosin--troponin under the experimental conditions. Some adsorption was evident, however, in the case of aspartate aminotransferase, (NADP) isocitrate dehydrogenase and alpha-glycerolphosphate dehydrogenase. 6. These results have been discussed in relation to their functional significance and the roles of enzyme compartmentation in the cell.
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PMID:On the association of glycolytic enzymes with structural proteins of skeletal muscle. 111 88

In the subcommissural organ (SCO) of the guinea pig, rat, golden hamster, and mouse the activity and distribution of enzymes related to the energy-supplying metabolism and of some marker enzymes of different cell organelles have been investigated by means of mostly modified histochemical methods. The results were compared with findings in the ciliated ependyma of the ventricular wall and with those in the ependyma of the choroid plexus of the third ventricle. In the ependymal part of the SCO only a moderate activity of hexokinase is observed in its specialized columnar cells whereas a high activity is present both in the ciliated ependyma and the choroid plexus. - The staining pattern of glucose-6-phosphatase is similar to that of hexokinase but this enzyme is found is the SCO only. - Likewise hexokinase, glycogen granules and enzymes related to glycogen metabolism (phosphoglucomutase, uridine-diphosphoglucose pyrophosphorylase, glycogen synthetase and phosphorylase) are regularly found most numerous and active in the nuclear and supra-nuclear area of the ependymal part. These enzymes are less active in both the other ependymal regions. - Uridine-diphosphoglucose dehydrogenase could not be demonstrated in the SCO. The NADP-linked enzymes of the pentose phosphate shunt, glucose-6-phosphate and 6-phosphogluconate dehydrogenase, show a moderate activity which decreases also from the nuclear towards the apical area of the ependymal cells of the SCO. Enzymes of the glycolytic pathway, such as glucosephosphate isomerase, fructose-6-phosphate kinase, fructose-I,6-diphosphate aldolase, glyceraldehyde-3-phosphate and lactate dehydrogenase, are highly active in the SCO and are located mainly in the supranuclear area, too. Fructose-1,6-diphosphatase could not be demonstrated thus indicating that in the SCO the pathway is most probably only glycolytic but not gluconeogenetic. Compared to the ependyma of the ventricular wall and of the choroid plexus, in the SCO the M type subunits of lactate dehydrogenase predominate. Glycolytic enzymes are also very active in the choroid plexus but less in the ciliated ependyma. Compared to the ciliated ependyma and especially to the ependyma of the choroid plexus, the activities of enzymes which are only present in mitochondria (NAD-linked isocitrate dehydrogenase, succinate dehydrogenase, NAD-linked malate dehydrogenase after preextraction, cytochrome oxidase, 3-hydroxybutyrate and glycerolphosphate and glutamate dehydrogenase) are relatively low. Mitochondria are accumulated near the superior pole of the nuclei as well as in the most apical part of the ependymal cells. - The staining pattern of NADP-linked isocitrate and malate dehydrogenase as well as of NADH dehydrogenase suggests that these enzymes are localized both in and out of mitochondria. The extramitochondrial activity of the first two enzymes might be localized in the cytosol. The extramitochondrial activity of NADH dehydrogenase might be localized in the endoplasmic reticulum...
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PMID:Enzymatic organization of the subcommissural organ. 123 49

In recent years, evidence has been accumulating that metabolic pathways are organized in vivo as multienzyme clusters. Affinity electrophoresis proves to be an attractive in vitro method to further evidence specific associations between purified consecutive enzymes from the glycolytic pathway on the one hand, and from the citric acid cycle on the other hand. Our results support the hypothesis of cluster formation between the glycolytic enzymes aldolase, glyceraldehydephosphate dehydrogenase, and triosephosphate isomerase, and between the cycle enzymes fumarase, malate dehydrogenase, and citrate synthase. A model is presented to explain the possibility of regulation of the citric acid cycle by varying enzyme-enzyme associations between the latter three enzymes, in response to changing local intramitochondrial ATP/ADP ratios.
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PMID:Clustering of sequential enzymes in the glycolytic pathway and the citric acid cycle. 239 1

Guinea pigs were exposed to electric field of 50 Hz in different times of day. Activity of aldolase and malate dehydrogenase in whole liver homogenate as well as in nuclear, mitochondrial and supernatant liver fractions of guinea pigs was examined. A remarkable increase in enzyme activity in all studied groups was observed which may prove that a relevant electric stimulus can result in certain disorders in carbohydrate changes in liver cells.
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PMID:[Effect of electric fields on the living organism. III. Activity of fructose-1,6-diphosphate aldolase and malate dehydrogenase in whole liver homogenate and in subcellular liver fractions in guinea pigs]. 239 9

Brass splinters weighing 28 mg were implanted in the center of the vitreous of rabbit eyes. After a few days the well-known infiltration and liquefaction of the vitreous body were observed, together with retinal necrosis. Cellular and lysosomal enzymes usually found only in very low concentrations in the vitreous body increased more than a hundredfold during the inflammatory process and the increasing opacification. The enzymes assayed were lactic dehydrogenase (LDH), phosphofructose aldolase (ALD), glycerinaldehyde phosphate dehydrogenase (GAPDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G-6-PDH), glutathione reductase (GR), beta-N-acetylglucose aminidase (NAcGA), and cathepsin-D. The kinetics of enzyme reproduction in the vitreous suggested that the cellular enzymes of the energy producing metabolism might originate both from the invading leukocytes as well as from the degrading retina. It seems likely that the cathepsin-D occurring in the vitreous originates mainly from the retina, and the beta-N-acetylglucose aminidase mainly from the pigment epithelium. The pathologically increased enzyme activity might well permit diagnostic conclusions concerning the intensity and stage of destruction of the retina by brass poisoning.
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PMID:[Enzyme activities of the retina and vitreous body following experimental implantation of a brass splinter]. 262 23

The proteins of soybean roots undergoing anaerobiosis can be grouped into three classes. Class 1 proteins are induced severalfold and at least 28 of these were identified by in vivo labeling. These proteins include the enzymes alcohol dehydrogenase (ADH), fructose aldolase, pyruvate decarboxylase, phosphoglucomutase, and lactate dehydrogenase. Class 2 proteins include such enzymes as glucose phosphate isomerase, sucrase, and malate dehydrogenase; their specific activity remains constant in aerobiosis or anaerobiosis. The third class of proteins includes those enzymes such as peroxidase whose activity decreases more than 90% after just 1 day in anaerobiosis. Immunoblotting coupled with two-dimensional chromatography of in vitro translated plant extracts demonstrated that ADH level during anaerobiosis is controlled by its mRNA concentration. Little or no mRNA for ADH was detected in aerobically grown roots. This suggests that the increased level of ADH activity is due to de novo synthesis of the mRNA rather than activation of a sequestered mRNA or superactivation of the protein.
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PMID:Gene regulation during anaerobiosis in soya roots. 262 97

It is well established that caloric restriction extends life span and significantly retards the rate of occurrence of most age-associated degenerative disease processes. A paucity of data exists relative to the mechanisms by which caloric restriction accomplishes these events. We have examined the effect of caloric restriction in rats on several hepatic enzymes of intermediary metabolism. The activities of glycolytic and supporting enzymes including lactate dehydrogenase, pyruvate kinase, sorbitol dehydrogenase, and alcohol dehydrogenase were all decreased in response to caloric restriction. Fructose 1-phosphate aldolase and creatine phosphokinase were not altered. Likewise, enzymes associated with lipid metabolism (malic enzyme and glycerokinase) were reduced (fatty acid synthetase was reduced, but not to a statistically significant degree). Activities of enzymes supporting gluconeogenesis (glutamate oxaloacetate transaminase, tyrosine aminotransferase, glutamate pyruvate transaminase, glutamate dehydrogenase, amino acid oxidase, malate dehydrogenase, and glucose 6-phosphatase) were either unchanged or increased significantly by caloric restriction. Glucagon levels were decreased. Comparisons between young ad libitum fed and older calorically restricted rats revealed similar but not identical metabolic activity. These results suggest that caloric restriction produces an effect on intermediary metabolism, favoring the role of glucagon and glucose synthesis; but limiting the role of insulin and glucose catabolism in the liver. The former observation provides for the efficient support of peripheral tissues and the latter a level of energy production necessary only for self maintenance. Limited lipid metabolism suggests decreased potential for fatty acid epoxide formation and free radical damage to cellular macromolecules. Additionally, caloric restriction may delay the progressive age associated changes in the activities of some of the enzymes investigated.
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PMID:Effect of chronic caloric restriction on hepatic enzymes of intermediary metabolism in the male Fischer 344 rat. 266 33

A method for a 50-60-fold purification of a cysteine proteinase from trophozoites of Entamoeba histolytica using 35-80% ammonium sulphate fractionation, gel chromatography on Sephadex G-75, and preparative isoelectric focusing is described. The enzyme was examined for its proteolytic potencies towards native enzyme substrates. The amebic proteinase directly inactivates aldolase and glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle as well as glucose-6-phosphate dehydrogenase from yeast. The inactivation of citrate synthase from porcine heart proceeds rather slowly, whereas malate dehydrogenase from porcine heart is not affected by the amebic proteinase under the condition used. With the exception of aldolase all inactivated enzyme substrates have been cleaved by limited proteolyses yielding major cleavage products. The inactivation of aldolase probably functions by the release of a small segment from a terminus being essential for aldolase activity.
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PMID:Cysteine proteinase of Entamoeba histolytica. I. Partial purification and action on different enzymes. 287 Apr 30


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