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)

Interactions of glucose-6-phosphate isomerase (D-glucose-6-phosphate ketol-isomerase, EC 5.3.1.9), aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13), glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12), triose-phosphate isomerase (D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1), phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1), phosphoglycerate kinase (ATP:3-phospho-D-glycerate 1-phosphotransferase, EC 2.7.3), enolase (2-phospho-D-glycerate hydro-lyase, EC 4.2.1.11), pyruvate kinase (ATP:Pyruvate O2-phosphotransferase, EC 2.7.1.40) and lactate dehydrogenase [S)-lactate:NAD+ oxidoreductase, EC 1.1.1.27) with F-actin, among the glycolytic enzymes listed above, and with phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) were studied in the presence of poly(ethylene glycol). Both purified rabbit muscle enzymes and rabbit muscle myogen, a high-speed supernatant fraction containing the glycolytic enzymes, were used to study enzyme-F-actin interactions. Following ultracentrifugation, F-actin and poly(ethylene glycol) tended to increase and KCl to decrease the pelleting of enzymes. In general, the greater part of the pelleting occurred in the presence of both F-actin and poly(ethylene glycol) and the absence of KCl. Enzymes that pelleted more in myogen preparations than as individual purified enzymes in the presence of poly(ethylene glycol) and the absence of F-actin were tested for specific enzyme-enzyme associations, several of which were observed. Such interactions support the view that the internal cell structure is composed of proteins that interact with one another to form the microtrabecular lattice.
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PMID:Heteromerous interactions among glycolytic enzymes and of glycolytic enzymes with F-actin: effects of poly(ethylene glycol). 333 56

A procedure for the simultaneous purification to homogeneity of hexokinase, phosphoglucomutase 1 and 2, aldolase, phosphoglucose isomerase and glucose-6-phosphate dehydrogenase from human origin has been developed. Human placenta homogenate was first chromatographed on DE-52 column which retains hexokinase and glucose-6-phosphate dehydrogenase while the other enzymes are recovered in the unabsorbed protein fraction. The other steps in the purification involve Matrex gel and specific affinity chromatography for the DE-52 retained enzymes and phosphocellulose and Matrex gel chromatography for the other enzymes. All the enzymes mentioned were obtained in one week, with recoveries from 14 percent for glucose-6-phosphate dehydrogenase to 75 percent for hexokinase. Thus, the procedures utilized seem to be useful in obtaining large amounts of enzymes in a a homogeneous form from an easily available human tissue.
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PMID:Simultaneous preparation from human placenta of several enzymes of glucose metabolism. 337 5

Effect of naphthoquinone levels on the activity of enzymes involved in glycolysis and pentose phosphate cycles was studied in male rats. Under conditions of primary and secondary K-avitaminosis the enzymatic activity, limiting these cycles, (aldolase of fructose-1,6-diphosphate, glucose phosphate isomerase and glucose-6-phosphate dehydrogenase) was increased, while the mitochondrial glutamate dehydrogenase activity was decreased. As a result of metabolic transformations under conditions of K-avitaminosis (primary and secondary) concentration of DNA in the animal tissues was lowered.
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PMID:[The effect of vitamin K on the activity of glycolysis and pentose phosphate cycle enzymes]. 342 Aug 14

The high degree of constancy of enzyme catalytic activity in the plasma of a given individual is regulated by a complex system of flux equilibria consisting of eight basic processes. Some of these processes are of primarily theoretic importance. Enzymes from all tissues of the body, including the liver, are released via a continuous physiological process into the interstitial space and get into the intravascular space by way of lymphatic transport. The release of enzymes from tissues directly into the intravascular space is of secondary importance as is the exchange of enzyme molecules across capillary membranes from the intravascular to the interstitial space and vice versa. In contrast, enzymes from circulating blood cells are transported directly into the intravascular space. Enzymes are removed from the intravascular space at rates which vary greatly between both enzymes and species. In a review of the literature, half-lives of diagnostically important enzymes in plasma of man, dogs and rats were given and the striking differences in the results for a given enzyme are discussed from a methodological point of view. In a mathematical analysis, data for lymphatic transport of enzymes from dogs and rats (Lindena et al. (1986) this J. 24, 19-33) and of enzyme efflux from in vivo ageing erythrocytes (Lindena et al. (1986) this J. 24, 49-59) into the plasma are related to the elimination rate constants of enzymes from the plasma. The contribution of lymphatically transported enzymes to the basal catalytic activity in plasma (Lindena & Trautschold (1986) this J. 24, 11-18) amounts to 55-80% for lactate dehydrogenase and malate dehydrogenase, 80-90% for adenylate kinase and phosphohexose isomerase, 90-95% for aspartate aminotransferase and aldolase and 99% for creatine kinase. A model of Ca2+ -mediated vesicular transport of enzymes out of ageing erythrocytes is proposed. The importance of lymphatically transported enzymes to total plasma catalytic activity in dogs and rats argues for a similar contribution of lymph transport in man.
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PMID:Kinetic of adjustment of enzyme catalytic concentrations in the extracellular space of the man, the dog and the rat. Approach to a quantitative diagnostic enzymology, V. Communication. 351 20

In the mixed body lymph of the thoracic duct and in the defined organ lymph of the liver and the intestine, the catalytic activity concentrations of up to sixteen enzymes and the concentrations of albumin and protein were determined, as well as the transport rate of these substances and their lymph/plasma ratio. Thoracic duct lymph specimens were obtained from an extracorporeal lymph shunt in anaesthetized and conscious dogs and from short-term fistulas in anaesthetized rabbits, rats and mice. Additionally, rabbits and rats underwent passive motion of the hind limbs in another experimental trial. Thoracic duct flow in anaesthetized dogs is only half that seen in conscious dogs, due to bypassed muscular lymph. A similar flow change is seen during passive motion of hind limbs in anaesthetized rabbits and rats. From a literature review of flow in the four main lymphatics of the body, it is concluded that the thoracic duct flow should account for 50-70% of total body lymph flow. In the anaesthetized state, flow is mainly of visceral origin. In the conscious state and during passive motion the increased flow is of muscular origin. In the latter case, the catalytic activities of enzymes like lactate dehydrogenase, malate dehydrogenase, creatine kinase, aldolase and phosphohexose isomerase, increase in lymph as does their lymph/plasma ratio. These enzymes have high catalytic activities in muscle. Their transport into the blood increases 2-3-fold, due to a doubling of lymph flow. Reported data for anaesthetized and immobile animals therefore far underestimate the significance of thoracic duct enzyme transport. Liver lymph was obtained from anaesthetized dogs and rabbits. Our finding that lymph catalytic activity for several enzymes is higher than in plasma is not compatible with the proposed delivery of plasma proteins directly into the sinusoidal space without prior mixing with the Space of Disse. Enzymes in liver lymph should derive from parenchymal and endothelial lining cells. Their site of delivery from the hepatocyte seems different from that of proteins. Liver lymph is an important transport route of enzymes into the blood. Intestinal lymph was sampled from anaesthetized dogs, rabbits and rats. It was shown that most enzymes from the intestine are primarily released into the interstitial space and from there are transported via the lymph into the blood.
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PMID:Catalytic enzyme activity concentration in thoracic duct, liver, and intestinal lymph of the dog, the rabbit, the rat and the mouse. Approach to a quantitative diagnostic enzymology, II. Communication. 370 Dec 68

A method for determining Control Coefficients is proposed for systems studied in vitro and applied to a model pathway. Rat liver extract, which converts glucose into glycerol 3-phosphate, was used with the addition to the incubation mixture of fructose-bisphosphate aldolase, triose-phosphate isomerase and glycerol-3-phosphate dehydrogenase as 'auxiliary' enzymes, which leaves all the control on the first three enzymes. The flux of the metabolic pathway was recorded by assaying NADH decay. Flux Control Coefficients (CJE) of hexokinase, glucose-6-phosphate isomerase and phosphofructokinase were calculated by titration of the system with increasing quantities of extraneous enzymes. It is shown that the summation property is fulfilled. The applicability of this procedure to study the control in any metabolic pathway is discussed. Possible relevance of the method to conditions in vivo and its limitations are considered.
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PMID:Kinetics of metabolic pathways. A system in vitro to study the control of flux. 370 39

In three groups of healthy young subjects (n = 33; mean ages 6.4, 13.5, 17.1 years), muscle enzyme activities (creatine kinase, hexose phosphate isomerase, aldolase, pyruvate kinase, lactate dehydrogenase, citrate synthase, fumarase) of the vastus lateralis muscle were investigated to show age-dependent variations. A significant age-dependent increase in aldolase (P less than 0.05) and pyruvate kinase (P less than 0.01) activity and a decrease in fumarase activity (P less than 0.01) were computed. In relation to the age-dependent variation, maximum LDH activities could be measured at an age of 12-14 years; significantly decreased activities of the glycolytic enzymes could only be found in the youngest group.
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PMID:Skeletal muscle enzyme activities in healthy young subjects. 375 6

Enzymes of the Embden-Meyerhof-Parnas pathway and hexose monophosphate shunt were examined in cytoplasmic extracts of three serovars of Ureaplasma urealyticum. We found no glucose-6-phosphate or 6-phosphogluconate dehydrogenase, hexokinase, phosphoglucose isomerase, aldolase, or lactic dehydrogenase activities. We failed to find cytochrome pigments in extracts and found no significant production of 14CO2 from [U-14C]glucose, nor did we find oxygen-dependent reduced nicotinamide adenine dinucleotide oxidase activity. Lactic acid was found only at trace levels in spent culture fluids. Ureaplasmas are apparently nonfermentative and are unlike all other mollicutes in that they have no detectable oxygen-dependent reduced nicotinamide adenine dinucleotide oxidase activity.
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PMID:Metabolic distinctiveness of ureaplasmas. 379 29

The glycosomes of in vitro grown procyclic trypomastigote forms of Trypanosoma brucei were purified by three different procedures and the results compared by electron microscopy, enzyme assays and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Centrifugation on a self-forming Percoll gradient followed by a sucrose gradient centrifugation resulted in the least enriched glycosomal preparation. Centrifugation on a pre-formed Nycodenz gradient gave an improved preparation but the most homogeneous preparation of intact glycosomes was obtained after centrifugation on two successive sucrose gradients. Glycosomes purified by both the Nycodenz and double sucrose gradient procedures appeared larger than in situ glycosomes presumably due to an osmotic effect resulting from disruption of the granular matrix of the organelles. Nevertheless, there appears to be no loss of cisternal contents due to the swelling of the organelles. The glycosomes of the bloodstream form trypomastigotes purified by the same procedures show, however, no sign of swelling. A comparison of glycosomes purified from procyclic trypomastigotes and bloodstream form trypomastigotes prepared by the same double sucrose procedure demonstrated that in the glycosome of procyclic trypomastigotes: activities of hexokinase, phosphoglucose isomerase, phosphofructose kinase, aldolase and phosphoglycerate kinase and diminished by 80-100%; activities of glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and glycerol-3-phosphate dehydrogenase remain unchanged or are only slightly reduced; there is an appearance of four major new proteins, among which could be phosphoenol pyruvate carboxykinase and malate dehydrogenase. These observations are in basic agreement with those by Hart et al. (Mol. Biochem. Parasitol. 12, 25-35, 1984).
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PMID:An improved purification of glycosomes from the procyclic trypomastigotes of Trypanosoma brucei. 380 43

Serum levels of phosphohexose isomerase (PHI), aldolase (ALD) and hexokinase (HK) activities have been determined in 76 patients of carcinoma cervix, in search of proper diagnostic and prognostic parameters. All the three glycolytic enzyme levels studied were found to be significantly elevated in all the groups of malignancy and showed a relation to the clinical stage and tumor. Serum PHI levels were of best diagnostic significance even at an early stage of the disease. The enzyme levels correlated well with the prognosis of the disease.
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PMID:Diagnostic and prognostic significance of serum phosphohexose isomerase, aldolase and hexokinase in carcinoma cervix. 381 45


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