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 dermal cells in grey, xanthic, and white goldfish integuments were cytochemically characterized for the following enzymatic activities: tyrosinase, DOPA-oxidase, cytochrome oxidase, monoamine oxidase, peroxidase, non-specific esterase, cholinesterase, NAD-diaphorase, NADP-diaphorase, aryl sulfatase, nucleotide phosphodiesterase, beta-glucuronidase, acid phosphatase, alkaline phosphatase, adenosine triphosphatase, thiamine pyrophosphatase, glucose-6-phosphatase, aldolase, as well as succinate, malate, isocitrate, glutamate, glucose-6-phosphate, 6-phosphogluconate, alpha-glycerophosphate, alcohol, lactate, and beta-hydroxybutyrate dehydrogenases. It was found that the epidermis was a significant barrier to the access of cytochemical reaction substrates. Removal of the epidermal barrier provided dermal cell localizations of enzymatic activities which were reproducible. Further, alterations in reaction times and temperatures from the mammalian methodology provided conditions fe various integumental cells were compared for possible interrelationships. The basic foundations for future work with the dermis of poikilothermic vertebrates on an experimental basis were established. In addition, a previously undescribed non-pigmented dermal cell, the "x"-cell, was found to have enzymatic characteristics similar to both melanophores and lipophores. The "x"-cell may be the common precursor of both types of pigment cells.
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PMID:Cytochemical characterization of goldfish (Carassius auratus L.) dermis with special reference to the pigment cells. 82 86

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

Changes in the content of dipicolinic acid and mineral elements were studied in the process of Bacillus thuringiensis spore germination. The spores released up to 28% of dipicolinic acid and 18% of calcium at the activation stage, and 93 and 91%, respectively, at the initiation stage. At the same time, the content of Mg, Mn, Zn and P decreased while K, Na and Fe accumulated in the spores. The activities of total and serine proteases, alkaline phosphatase, NADH dehydrogenase and aldolase increased in the extract of initiated spores. The content of glutamate decreased in the free amino acid pool as early as by the 30th second of the initiation stage.
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PMID:[Amino acid and mineral element content and the activity of various enzymes in germinating spores of Bacillus thuringiensis]. 389 44

The series introduced by this paper reports the results of a detailed analysis of the microsomal fraction from rat liver by density gradient centrifugation. The biochemical methods used throughout this work for the determination of monoamine oxidase, NADH cytochrome c reductase, NADPH cytochrome c reductase, cytochrome oxidase, catalase, aminopyrine demethylase, cytochromes b(5) and P 450, glucuronyltransferase, galactosyltransferase, esterase, alkaline and acid phosphatases, 5'-nucleotidase, glucose 6-phosphatase, alkaline phosphodiesterase I, N-acetyl-beta-glucosaminidase, beta-glucuronidase, nucleoside diphosphatase, aldolase, fumarase, glutamine synthetase, protein, phospholipid, cholesterol, and RNA are described and justified when necessary.
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PMID:Analytical study of microsomes and isolated subcellular membranes from rat liver. I. Biochemical methods. 415 Apr 88

Rat liver microsomal fractions have been equilibrated in various types of linear density gradients. 15 fractions were collected and assayed for 27 constituents. As a result of this analysis microsomal constituents have been classified, in the order of increasing median density, into four groups labeled a, b, c, and d. Group a includes: monoamine oxidase, galactosyltransferase, 5'-nucleotidase, alkaline phosphodiesterase I, alkaline phosphatase, and cholesterol; group b: NADH cytochrome c reductase, NADPH cytochrome c reductase, aminopyrine demethylase, cytochrome b(5), and cytochrome P 450; group c: glucose 6-phosphatase, nucleoside diphosphatase, esterase, beta-glucuronidase, and glucuronyltransferase; group d: RNA, membrane-bound ribosomes, and some enzymes probably adsorbed on ribosomes: fumarase, aldolase, and glutamine synthetase. Analysis of the microsomal fraction by differential centrifugation in density gradient has further dissociated group a into constituents which sediment more slowly (monoamine oxidase and galactosyltransferase) than those of groups b and c, and 5'-nucleotidase, alkaline phosphodiesterase I, alkaline phosphatase, and the bulk of cholesterol which sediment more rapidly (group a2). The microsomal monoamine oxidase is attributed, at least partially, to detached fragments of external mitochondrial membrane. Galactosyltransferase belongs to the Golgi complex. Group a2 constituents are related to plasma membranes. Constituents of groups b and c and RNA belong to microsomal vesicles derived from the endoplasmic reticulum. These latter exhibit a noticeable biochemical heterogeneity and represent at the most 80% of microsomal protein, the rest being accounted for by particles bearing the constituents of groups a and some contaminating mitochondria, lysosomes, and peroxisomes. Attention is called to the operational meaning of microsomal subfractions and to their cytological complexity.
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PMID:Analytical study of microsomes and isolated subcellular membranes from rat liver. 3. Subfractionation of the microsomal fraction by isopycnic and differential centrifugation in density gradients. 415 Apr 90

Cells of the aerotolerant anaerobe Giardia lamblia respire in the presence of oxygen. Endogenous respiration is stimulated by glucose but not by other carbohydrates and Krebs cycle intermediates. Endogenous and glucose-stimulated respiration are insensitive to cyanide, malonate, and 2,4-dinitrophenol, but are inhibited by atabrin and iodoacetamide. G. lamblia produces ethanol, acetate and CO2 both aerobically and anaerobically either from endogenous reserves or exogenous glucose. Molecular hydrogen is not produced. The following enzyme activities were detected in homogenates: hexokinase, fructose-biphosphate aldolase, pyruvate kinase, phosphoenolpyruvate carboxykinase, malate dehydrogenase, malate dehydrogenase (decarboxylating), pyruvate synthase, acetyl-CoA synthetase, alcohol dehydrogenase (NADP+), NADH dehydrogenase, NADPH dehydrogenase, NADPH oxidoreductase and superoxide dismutase. The enzymes of energy and carbohydrate metabolism are nonsedimentable (109 000 x g for 30 min). Activities of lactate dehydrogenase, hydrogenase, phosphate acetyltransferase, acetate kinase, citrate synthase, succinate dehydrogenase, fumarate hydratase and catalase were below the limits of detection. The results suggest the occurrence of glycolysis, energy production by substrate level phosphorylation and a flavin, iron-sulfur protein mediated electron transport system as well as the absence of cytochrome mediated oxidative phosphorylation and functional Krebs cycle.
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PMID:Energy metabolism of the anaerobic protozoon Giardia lamblia. 610 7

Injection of leupeptin (an inhibitor of lysosomal cathepsins B, H, and L) to nonstarved rats causes an expansion of the autophagic vacuolar (AV) system in hepatocytes. Readily identifiable cytoplasmic constituents were seen within the AVs shortly after the administration. Later, the contents of the AVs seemed to reach more advanced stages of degradation. Liver AVs were purified by a one-step centrifugation of a crude mitochondrial lysosomal fraction in a discontinuous metrizamide gradient after exposing the rats to leupeptin for varying periods of time. Leupeptin caused alterations of the AV fraction that were time dependent. Initially, i.e., after 30 minutes of leupeptin exposure, mature (secondary) lysosomes clearly dominated over nascent AVs. The situation was reversed when fractionation was performed 1 or 2 hours following the injection of leupeptin. Now, the AVs were more frequent than the mature lysosomes. Later, the proportion of mature lysosomes was again larger. An increase in dense bodies was noted after 16 hours of leupeptin treatment. The proteolytic capacity of the AVs at different stages of maturation was measured after labeling liver proteins with an injection of L-1-14C-leucine 16 hours before sacrifice. AVs were purified after varying times of exposure to leupeptin. The proteolysis decreased greatly 1 to 2 hours following the injection of leupeptin but never ceased. On the other hand, lipolysis seemed unaffected by leupeptin using a similar experimental protocol as for proteolysis. If the animals were subjected to more lasting exposure to leupeptin before fractionation, proteolysis increased, displaying a peak higher than control, occurring after approximately 4 hours. The degradation gradually returned to control values after 16 hours. A catch-up in proteolysis was thus observed. The time course of proteolysis was reflected in the protein content in the AV fraction. After an initial increase that coincided with the lowered proteolysis, it returned to control level. Marker enzyme activities for endoplasmic reticulum and mitochondria (G6Pase and succinate-cytochrome c reductase) followed the same pattern. The AV content of the cytosolic enzymes lactate dehydrogenase and aldolase reached as high as 2.30 and 2.80% of the values in the homogenate during the 1st hour of leupeptin exposure. From these data the half-lives of the enzymes were calculated. They were: for aldolase, 43 hours; for LDH, 68 hours. This suggests that AVs account for a substantial proportion of degradation not only of organelles but also of soluble cytosolic enzymes.
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PMID:Effect of leupeptin on the autophagic vacuolar system of rat hepatocytes. Correlation between ultrastructure and degradation of membrane and cytosolic proteins. 633 Apr 53

The activity of endocellular enzymes (alkaline phosphatase, protease, glucose dehydrogenase, aldolase, malate dehydrogenase, NADH dehydrogenase, NADH oxidase) was studied in isolated prospores and sporangia as well as in vegetative cells of Bacillus thuringiensis strains, one of which produced crystals and one did not. The activity of malate dehydrogenase and NADH dehydrogenase was high in prospores of the both strains at the fifth and sixth stages of spore formation. The strain which did not produce crystals differed from the parent strain by a higher aldolase activity at all of the growth stages and by an abrupt increase in the activity of hydrolytic enzymes in sporangia (in the cytoplasm of the parent cells).
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PMID:[Activity of intracellular enzymes in Bacillus thuringiensis prospores and sporangia]. 634 86

Changes in the activity of 13 enzymes are described in the process of cytodifferentiation of the nerve cells of spinal ganglion, the motor neurons of spinal cord and large nerve cells of the III layer of tectum opticum in 7, 10 and 21 day old chick embryos. Cytophotometry was performed with MZFV-1 (LOMO) by means of plug-method. A relatively high activity of glucose-6-phosphat dehydrogenase, diaphorase, alpha-glycerophosphate dehydrogenase and, partially, acetylcholine esterase was found already in the 7 days old embryo. The activity of monoamine oxidase, aldolase-glyceroaldehyde phosphate dehydrogenase, isocitrate dehydrogenase, glutamate dehydrogenase increased markedly on the 21st day. When studying the reciprocal distribution of two enzymes in separate cells, pairs of enzymes with a high value of correlation coefficient were found. The cytodifferentiation was found to be accompanied by changes in the coefficient of correlation of the same pair of enzymes.
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PMID:[Enzymes in the process of neuronal differentiation of the hen spinal ganglion, spinal cord and tectum opticum. A cytophotometric histochemical study]. 683 47

The energy metabolism of the English E-CMO strain of contagious equine metritis bacterium was studied in whole cells and cell extracts. This bacterium appears to have an active Krebs cycle and probably obtains energy by oxidative phosphorylation since glycolysis and the hexose monophosphate pathways appear to be absent. These conclusions are based on the findings that [U-14C]glucose incorporation by this bacterium is below the level of detection, and that respiration is stimulated by Krebs cycle intermediates (i.e., malate, citrate, and succinate), but not by glucose, fructose, maltose, or sucrose. Furthermore, support comes from the fact that enzymes generally associated with the Krebs cycle and electron transport (i.e., malate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase, fumarate hydratase, malate dehydrogenase [decarboxylating], cytochrome oxidase, superoxide dismutase, NADH dehydrogenase, and catalase) were detected. Those enzymes normally associated with glycolysis and the hexose monophosphate pathways (i.e., hexokinase, glucose 6-phosphate dehydrogenase, fructose biphosphate aldolase, glycerol 3-phosphate dehydrogenase, phosphoenolpyruvate carboxykinase, pyruvate kinase, phosphate acetyl transferase, acetate kinase, alcohol dehydrogenase, and lactate dehydrogenase) were below the level of detection.
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PMID:Energy metabolism of the contagious equine metritis bacterium. 708 71


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