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)

Histochemical studies were carried out on some of the glycolytic enzymes viz. phosphorylase, aldose, alpha-glycerophosphate dehydrogenase (alpha-GPDH) and lactic dehydrogenase (LDH) and a key enzyme of the pentose phosphatase cycle, glucose-6-phosphate dehydrogenase (G-6-PDH), in the hepatopancreas of Scylla serrata (Forskal). 1. Weak activities of phosphorylase and aldolase and strong-activities of alpha-GPDH and LDH were noticed mainly in the brush border of the tubules and R-cell cytoplasm. A trace activity of G-6-PDH was noticed in the brush border. 2. Bilateral eyestalk removal results in inhibition of both phosphorylase and aldolase. However, enhanced activities of alpha-GPDH and LDH were noticeable 4 h after the operation. The G-6-PDH activity remained unaltered till 24 h. 3. Injection of eyestalk extract into both intact and destalked crabs activated all the enzymes.
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PMID:Histochemical observations on the occurrence of glycolytic and pentose phosphate cycle enzymes in the hepatopancreas and their possible relation to eyestalk factor(s) in the crab Scylla serrata (Forskal). 0 Aug 64

1. Procedures were developed for the extraction and assay of glycolytic enzymes from the epididymis and epididymal spermatozoa of the rat. 2. The epididymis was separated into four segments for analysis. When rendered free of spermatozoa by efferent duct ligation, regional differences in enzyme activity were apparent. Phosphofructokinase, glycerol phosphate dehydrogenase and glucose 6-phosphate dehydrogenase were more active in the proximal regions of the epididymis, whereas hexokinase, lactate dehydrogenase and phosphorylase were more active in the distal segment. These enzymes were less active in the epididymis of castrated animals and less difference was apparent between the proximal and distal segments. However, the corpus epididymidis from castrated rats had lower activities of almost all enzymes compared with other epididymal segments. 3. Spermatozoa required sonication to obtain satisfactory enzyme release. Glycolytic enzymes were more active in spermatozoa than in epididymal tissue, being more than 10 times as active in the case of hexokinase, phosphoglycerate kinase and phosphoglycerate mutase. 4. The specific activities of a number of enzymes in the epididymis were dependent on the androgen status of the animal. These included hexokinase, phosphofructokinase, aldolase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, pyruvate kinase, glycerol phosphate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and phosphorylase. 5. The caput and cauda epididymidis differed in the extent to which enzyme activities changed in response to an altered androgen status. The most notable examples were hexokinase, phosphofructokinase, aldolase, phosphoglycerate kinase, 6-phosphogluconate dehydrogenase and phosphorylase.
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PMID:Activity and androgenic control of glycolytic enzymes in the epididymis and epididymal spermatozoa of the rat. 18 56

An ultramicrochemical technique has been adapted to the evolution of enzyme profiles within individual human mammary tumors. Tandem observation of adjacent stained and lyophilized sections permitted dissection of microgram quantities of freeze-dried material within confirmed regions of malignancy. Enzymes frequently monitored to examine glycolytic, respiratory, and metastatic capacity were microanalyzed successfully: lactic dehydrogenase (LDH), phosphoglucose isomerase (PGI), malate dehydrogenase (MDH), acid phosphatase (AP), aldolase (ALD), glucose-6-phosphate dehydrogenase (G6PDH), pyruvate kinase (PK), alpha-glycerophosphate dehydrogenase (alpha-GOPDH), hexokinase (HK), and phosphofructokinase (PRK). All enzyme activities were higher in infiltrating ductal carcinomas than in fibroadenomas. Extracts of tumor cells mixed in varying proportions with brain or muscle extracts of rat evidenced no modification of expected activity. The technical adaptation described provided a sensitive methodology to resolve problems of relication, profile analysis, sample quantity, and selectivity within heterogeneous tissues.
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PMID:Application of a microchemical technique to the elucidation of enzyme activity profiles within single human mammary tumors. 20 41

Eschscholtzia californica stigmas with germinating pollen at different stages of development were the subject of histochemical studies which aimed the localization of several enzymes like phosphorylase, leucine amino peptidase, nonspecific esterase, cytochrome oxidase, aldolase, alpha-glycerophosphate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, monoamine oxidase, alpha-galactosidase, beta-glucosidase and beta-galactosidase. Pollen and pollen tubes were shown to contain starch, lipid, proteins and soluble sugars as the storage products. These storage products were utilized during germination and tube growth. The role of different enzymes in the process of germination and tube growth is discussed. From the distribution of oxidoreductases it is inferred that respiration plays an essential role in the tube growth. During pollen germination probably the reserve proteins were transported to pollen tube tip. The increase of activity of alpha-and beta-galactosidase in pollen tubes indicates on their involvement in carbohydrate metabolism. The role of alpha-galactosidase in the metabolism of galactolipids is also inferred. Similarly, the reaction catalysed by beta-glucosidase resulted in the production of aglycon and glucose; of these the former possibly act as a substrate of peroxidase. Some of the glycosidases diffused out of pollen wall on the stigma and participated in the release of free sugars of the female tissue.
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PMID:Studies on the physiology of pollen and pollen tube growth. IV Eschscholtzia californica Cham. 22 Jan 58

3-Hydroxy-4-oxobutyl-1-phosphonate, the phoshonic acid analogue of glyceraldehyde 3-phosphate, enters Escherichia coli via the glycerol 3-phosphate transport system. There is no differential effect upon the accumulation of deoxyribonucleic acid, ribonucleic acid, or phosphoglycerides, although the accumulation of proteins was less effected. Examination of the phospholipids revealed that phosphatidylglycerol accumulation was most severely inhibited and cardiolipin accumulation was least affected. Concentrations of glyceraldehyde 3-phosphate and its phosphonic acid analogue that markedly inhibit macromolecular and phosphoglyceride biosynthesis have no effect upon the intracellular nucleoside triphosphate pool size. The phosphonate is a competitive inhibitor of sn-glycerol 3-phosphate in reactions catalyzed by acyl coenzyme A:sn-glycerol-3-phosphate acyltransferase and CDP-diacylglycerol:sn-glycerol-3-phosphate phosphatidyltransferase. A Km mutant for the former enzyme was susceptible to the phosphansferase activity. Studies with mutant strains ruled out the aerobic glycerol-3-phosphate dehydrogenase, glycerol-3-phosphate synthase, and fructose-1,6-biphosphate aldolase as the primary sites of action.
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PMID:Glycerol 3-phosphate analogues as metabolic inhibitors in Escherichia coli, 3-hydroxy-4-oxobutyl-1-phosphonate, a drug that interferes with normal phosphoglyceride metabolism. 37 6

Detailed histochemical studies have been conducted on the distribution of various enzymes, including thiamine pyrophosphatase, alpha-glucan phosphorylase, hexokinase, glucose-6-phosphate dehydrogenase, aldolase, glycerol-3-phosphate dehydrogenase; menadion oxidoreductase, lactate dehydrogenase and succinate dehydrogenase in various components of the cerebellum of healthy adult male rats of the Wistar strain. The thiamine pyrophosphatase reaction showed the morphological patterns of the GOLGI apparatus characteristic for each kind of cells. The GOLGI apparatus is a simple network in stellate cells, but it can be classified into the same 5 categories in basket cells and GOLGI type II cells. The GOLGI apparatus in the latter 2 cell types appears to undergo cyclic changes. A few GOLGI type II cells have a supranuclear form (Type II) and some cells show disintegration and "budding-off" of the GOLGI apparatus. The GOLGI apparatus in PURKINJE cells can be classified into 4 categories including a perinuclear strand form (Type III), but most of them show randomly distributed granules and vesicles. Lightly stained networks are observable in astrocytes and oligodendrocytes. They do not show polarity in astrocytes whereas they have extensions in a few oligodendrocytes. BERGMANN glia may undergo cyclic changes indicating more advance differentiation than astrocytes and oligodendrocytes. Cerebellar glomerula show lightly stained networks with many fine granules. Granule cells, stellate cells, and basket cells are all poorly equipped equally with the EMBDEN-MEYERHOF (EM) pathway and with the hexosemonophosphate (HMP) shunt. GOLGI type II cells are richly equipped almost equally with both the EM pathway and the HMP shunt. All these neurons probably derive energy mainly from glucose in the circulating blood. PURKINJE cells may belong to the category of "usual neurons", because they are moderately equipped both with the EM pathway and the HMP shunt. However, they may derive their energy from the BERGMANN glia which have intense hexokinase activity but weak succinate dehydrogenase activity. The BERGMANN glia are more richly equipped with the HMP shunt than with the EM pathway and are rich in lactate dehydrogenase suggesting an "exceptional metabolic pattern". These glia may have active synthesizing ability. Astrocytes and oligodendrocytes are equipped with all the enzymes tested, and they show a tendency to surround the glomeruli. It is suggested that the glomerula may be surrounded by the glial sheaths with strong hexokinase activity, and that they may contain alpha-glucan phosphorylase, glucose-6-phosphate dehydrogenase, and glycerol-3-phosphate dehydrogenase in addition to the succinate dehydrogenase already reported. A few PURKINJE cells showed perinuclear concentrations of the reaction product only of succinate dehydrogenase at the sites of contacts between nucleoli and nuclear membranes. It is suggested that the nucleolus may receive adenosine at the sites of contacts between nucleoli and nuclear membranes...
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PMID:Histochemical studies on the morphology of the Golgi apparatus and on the distribution of some enzymes concerned with carbodydrate metabolism in the rat cerebellum. 40 26

Extracts of the horse and sheep strains of Echinococcus granulosus and E. multilocularis were compared on the basis of their isoenzyme patterns for 10 enzymes by means of isoelectric focusing in polyacrylamide gels. The enzymes examined were: acid phosphatase, lactate dehydrogenase, malate dehydrogenase, malic enzyme, phosphoglucoseisomerase, isocitrate dehydrogenase, adenylate kinase, aldolase and alpha-glycerophosphate dehydrogenase. Interspecific and intraspecific differences are apparent in the isoenzyme profiles of all the enzymes except adenylate kinase; the pattern and activity of adenylate kinase are identical for both strains of E. granulosus but this enzyme clearly distinguishes these forms from E. multilocularis. The absence of electromorphic variation in any of the enzymes from either form of E. granulosus may be a result of the self-fertilizing hermaphraditism of these organisms.
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PMID:Isoelectric focusing of some enzymes from Echinococcus granulosus (horse and sheep strains) and E. multilocularis. 47 21

Hexokinase, aldolase, L-alpha-glycerophosphate dehydrogenase, and lactate dehydrogenase activities were determined in the kidney of the aging cat. Kidneys from 24 domestic cats 2 months to 7.5 years old in 6 age groups were examined by light microscopic and histochemical methods. Enzyme activities in anatomic components of the kidney were assessed on a quantitative basis for evaluation of mean activity between the age groups. In the cats with advancing age, renal components generally had stable activity. A significant (P less than 0.05) increase in hexokinase activity occurred with advancing age in the ascending part of the renal loop (Henle's loop) and in the distal convoluted tubule. Significant (P less than 0.05) increases in aldolase activity with aging were in cortical connective tissue, internal part of the glomerular capsule (podocytes), distal convoluted tubule, and convoluted segment (Pi) of the proximal portion of the nephron tubule. L-alpha-glycerophosphate dehydrogenase and lactate dehydrogenase activity increased significantly with aging in the convoluted (Pi) segment of the proximal portion of the nephron tubule.
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PMID:Kidney in the aging cat: hexokinase, aldolase, L-alpha-glycerophosphate dehydrogenase, and lactate dehydrogenase histochemistry. 69 42

The enzymatic analysis of fructose-1,6-diphosphate by a coupled assay utilizing triose-phosphate isomerase, glycerol-3-phosphate dehydrogenase and aldolase was carried out in rat serum and human plasma after fructose-1,6-diphosphate administration. The rate of disappearance of fructose-1,6-diphosphate was determined and compared to the activity of aspecific phosphatase. The uptake of fructose-1,6-diphosphate by rat liver and ileum was also determined with the same method.
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PMID:Enzymatic assay of fructose-1,6-diphosphate for the measurement of its utilization by tissues. 84 54

Soluble enzymes were immobilized and visualized by polyacrylamide gel slabs, impregnated with the incubation medium including auxiliary enzymes. The method has several advantages over existing techniques which make use of gel films or a semipermeable membrane. The diffusion of tissue compounds is effectively limited, while auxiliary enzymes may be operative. Moreover the viscosity of the medium is temperature-independent so that the incubation temperature can be varied. To demonstrate the suitability of the method glycerol-3-phosphate dehydrogenase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, hexokinase, phosphoglucomutase and aldolase were visulaized in human or rat skeletal muscle. Cytosolic and mitochondrial glycerol-3-phosphate dehydrogenase were both visualized in the absence of added NAD+ and menadione. For the visualization of ATP producint enzymes, like creatine kinase and pyruvate kinase, the method is not suitable.
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PMID:Polyacrylamide gel technique for the histochemical demonstration of soluble enzymes. 105 94


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