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)

This paper starts a series on red blood cell (RBC) metabolism in patients with chronic renal failure (CRF). The glycolytic enzyme levels and in vitro half-lives of these patients' RBCs were determined. A number of enzymes (hexokinase, glucose-6-phosphate isomerase, fructose-6-phosphate kinase, aldolase, glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase) showed higher activities than in normal control RBCs. Other enzyme activities were normal. These results were discussed and several possible mechanisms considered. We favour the point of view of a shortened life span of the RBCs in CRF, making the most unstable enzymes of the glycolytic sequence appear increase as compared with normal controls.
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PMID:Metabolism of red blood cells in chronic renal failure. I. Glycolytic enzyme levels. 22 98

The concept of tumor markers was reviewed, and the potential uses of markers of central nervous system (CNS) tumors and methods for their evaluation were discussed. Markers examined included lactate dehydrogenase, aspartate aminotransferase, fructose-bisphosphate aldolase, the polyamines, desmosterol, and several other enzymatic, nonenzymatic, and immunologic markers. Data collated from the clinical studies surveyed showed isocitrate dehydrogenase, desmosterol, and the polyamines to have the greatest potential utility in the diagnosis of CNS tumors.
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PMID:Biochemical markers of central nervous system tumors measured in cerebrospinal fluid and their potential use in diagnosis and patient management: a review. 38 10

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

The hepatocyte and haematopoietic cell contents of the liver of the foetal guinea pig were measured over the latter half of gestation. Hepatocytes represented about 30% of liver volume at mid-gestation and this increased to 70-80% by term; cell volume remained fairly constant until 5-7 days before term, then more than doubled. Haematopoietic cells represented about 5% of liver volume at mid-gestation and this progressively fell to <1% by term. At 75% of gestation hepatocytes and haematopoietic cells were prepared from perfused foetal livers by collagenase digestion. Enzyme activity of the hepatocyte was, without exception, similar to that of the whole liver. In general, enzyme activity in the haematopoietic cells was similar to that in erythrocytes, with relatively low values for aldolase, glycerol 3-phosphate dehydrogenase, phosphoglycerate mutase, enolase, lactate dehydrogenase, phosphoenolpyruvate carboxykinase, fructose 1,6-bisphosphatase, isocitrate dehydrogenase, ;malic' enzyme, glutamate dehydrogenase and aspartate aminotransferase. The haematopoietic cell contribution to total enzyme activity in the foetal liver was usually much less than 10% and could thus not account for the major changes in hepatic enzyme activity over the latter half of gestation. Hepatocytes contained hexokinase isoenzymes I and III, aldolase isoenzymes A and B and pyruvate kinase isoenzymes 1, 2 and 4. The haematopoietic cells contained hexokinase isoenzyme I and two additional bands of activity with slightly greater mobility, aldolase isoenzyme A and pyruvate kinase isoenzymes 2 and 4.
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PMID:The distribution of enzyme and isoenzyme activities between parenchymal and haematopoietic cells in the liver of the foetal guinea pig. 43 88

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

Various enzymes of glycolysis (hexokinase, phosphoglucoisomerase, aldolase and lactate dehydrogenase), the Krebs cycle (isocitrate, succinic and malate dehydrogenases), and the pentose phosphate cycle (glucose-6-phosphate and 6-phosphogluconate dehydrogenases) were studied in buffalo spermatozoa by biochemical and cytochemical methods. The enzymes of glycolysis were found to be loosely bound whereas those of the Krebs and pentose phosphate cycles were strongly bound to mitochondrial membranes. All the enzymes studied were localized histochemically in the mid-piece.
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PMID:Glycolytic, Krebs cycle and pentose phosphate cycle enzymes in spermatozoa of the buffalo (Bubalus bubalis). 51 3

Studies on organ homogenates of 22 one-year-old healthy geese indicated ubiquiternal distribution of GOT and GPT transaminases, lactate dehydrogenase, alkaline and acid phosphatase, aldolase and kreatine phosphokinase, without the presence of any pronounced organ specificity of some of the named enzymes. It is presumed that the investigation on these enzymes in goose blood serum can be of use only for determining the degree and the course of a given disease, but not for organ-localization of the disease's process.
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PMID:[Enzymatic activity study of the organs and blood serum of geese]. 53 93

The present study was designed to analyze the effects of a short term stress on the quantitative levels of alkaline phosphatase (AP), creatine phosphokinase (CK), aldolase (ALD), lactate dehydrogenase (LDH), and lactate dehydrogenase-1-isoenzyme (LDH 1) during 24 h after stress. For all the enzymes studied higher values for the activity were found due to stress in comparison to the activity level before the stress. The period during the 24 h after stress to reach maximum activity depends on the enzyme and in part on the sex of the animal.
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PMID:[Effects of a definite stress on the enzyme activities in blood plasma in mice (author's transl)]. 57 Jan 20

The changes in the sarcoplasmic proteins of the m. gastrocnemius and m. soleus were examined by biochemical methods on the 5th, 7th, 14th and 28th days after plaster cast immobilization of the right hind limbs of adult rabbits. During 4 weeks the soluble/myofibrillar protein ratio increased from 0.47 to 0.75 in the m. gastrocnemius, and to 0.85 in the m. soleus. Evaluation of the relative quantities of the components identified after gel-electrophoresis separation led to the following results: (1) There was no, or no appreciable change in the glyceraldehyde-3-phosphate dehydrogenase, creatine kinase and enolase activities. (2) The enzymes lactate dehydrogenase, aldolase and the glycogenolytic enzymes showed a relative decrease in both muscles. (3) Phosphoglycerate kinase, phosphoglucose isomerase and pyruvate kinase increased in both muscles. (4) Changes of opposite directions were exhibited by myoglobin, myokinase and F-protein. These results provide new data on the biochemical characterization of these functionally different muscles, and on the mechanism of disuse atrophy.
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PMID:Experimental investigations on hypokinesis of skeletal muscles with different function. IV. Changes in the sarcoplasmic proteins. 60 15

Several glycolytic enzymes were observed to have between 40-90% of their activities associated with the particulate fractions of lysed nerve endings. The enzymes showing high particulate activity in lysed nerve endings were hexokinase (EC 2.7.1.1), aldolase (EC 4.1.2.13), glucosephosphate isomerase (EC 5.3.1.9), phosphofructokinase (EC 2.7.1.11), glyceraldehyde-phosphate dehydrogenase (EC 1.2.1.12), pyruvate kinase (EC 2.7.1.40) and lactate dehydrogenase (EC 1.1.27). With the exception of phosphofructokinase, 80% or more of the particle associated activity of each enzyme was solubilized by salt treatment indicating the association with particles was ionic. Sub-fractionation of lysed nerve endings showed hexokinase and fumarase (EC 4.2.1.2) had the highest specific activity in the same fractions which is consistent with observations indicating that hexokinase is associated with mitochondria. The other glycolytic zymes having high particulate activity, aldolase, glucosephosphate isomerase, phosphofructokinase, glyceraldehyde-phosphate dehydrogenase, pyruvate kinase and lactate dehydrogenase, showed enrichment in fractions containing synaptosomal membranes, i.e. the fractions having highest specific activity of acetylcholinesterase (EC 3.1.1.7) and (Na+ + K+)-ATPase (EC 3.6.1.3).
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PMID:Association of glycolytic enzymes with particulate fractions from nerve endings. 62 35


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