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)

In order to identify and to characterize the antigens from Nippostrongylus brasiliensis which are involved in the in vitro blastogenesis of T cells from infected animals, we have established by crossed immunoelectrophoresis a two dimensional antigenic map of the adult worm homogenate. Polyclonal precipitating rabbit antiserum recognized 26 antigens including five enzymes in these homogenates. The antigenic enzymes, the precipitates of which are only stained by specific staining, are: aldolase, malic enzyme, acid phosphatase, peroxydase and cholinesterase. This antigenic map enable us to identify 26 antigens in adult worm homogenates and to compare them with those which will be contained in purification fractions from these homogenates or in homogenates from other parasites.
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PMID:Antigenic analyses of the adult worms of Nippostrongylus brasiliensis by crossed immunoelectrophoresis. 409 83

Only intact exudate granulocytes from rabbits generated large amounts of endogenous pyrogen when incubated in 0.15 M NaCl. No matter how whole-cell lysates or combinations of subcellular fractions were incubated, their yields of pyrogen never approached those of whole cells; at most, only minimal amounts of pyrogen were formed, once the integrity of the cells had been destroyed. Some pyrogen could be extracted from disrupted cells, but never more than a fraction (<25%) of that released from incubated whole cells. The yield could be slightly improved by lowering the pH (to 3.5) and by increasing the volume of extraction fluid. Virtually all of the preformed pyrogen that could be extracted from sucroselysed cells was found in their cytoplasmic fraction. Contrary to the results of Herion et al. (3), none could be detected in the granular (or lysosomal) fraction. Likewise, all efforts to recover pyrogen from the membrane-nuclear fraction were unsuccessful. In keeping with the finding that preformed pyrogen is contained in the cytoplasmic fraction were the observations that practically all of the aldolase, a cytoplasmic enzyme, and very little of the acid phosphatase, a granular enzyme, were lost from the cells during the release of pyrogen. Lysozyme, an enzyme stored in both the granules and the cytoplasm, was partially released from the cells under the same circumstances. Neither the release of pyrogen nor its slight intracellular buildup that precedes release (4) were affected by concentrations of puromycin that block protein synthesis in the cells and prevent their activation. Hence, it is concluded that the release process, which also involves the formation of active pyrogen (4), does not require protein synthesis, whereas activation of the cells, which may involve the synthesis of an inactive precursor (2), does.
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PMID:Studies on the pathogenesis of fever. XIX. Localization of pyrogen in granulocytes. 543 Jul 84

Administration of leupeptin to rats induces the accumulation of numerous autophagic vacuoles in the liver. Furuno et al. (Furuno, K., Ishikawa, T., and Kato, K. (1982) J. Biochem. (Tokyo) 91, 1485-1494) have recently devised a method for Percoll density gradient equilibrium fractionation of crude lysosomal fractions to isolate a highly enriched preparation of autophagic vacuoles. This system was used to determine whether cytoplasmic enzymes are normally sequestered into autophagic vacuoles in fed animals. Within 30 min following the administration of leupeptin to fed rats, several cytoplasmic enzymes could be demonstrated in vacuolar fractions heavier than mitochondria and normal lyosomes. The activities of tyrosine aminotransferase and lactic dehydrogenase as well as antigens of fructose-bisphosphate aldolase were detectable in fractions with densities of 1.115 to 1.15 g/ml containing cathepsins and acid phosphatase. The cytoplasmic enzymes in these fractions exhibited latency and were sequestered within membranous organelles. Six hours after the administration of leupeptin, the autophagic vacuoles gradually disappeared from these fractions concurrently with the loss of both cytoplasmic and lysosomal marker enzymes. For 6 h after injection of leupeptin the activities of cathepsin D and acid phosphatase increased in autophagic vacuoles and decreased in the postvacuolar lysosomal fraction. Administration of dexamethasone, which induces the synthesis of tyrosine aminotransferase and cytosolic aspartate aminotransferase, selectively increased the sequestration of these enzymes to proportional degrees. Cycloheximide administered simultaneously with leupeptin rapidly inhibited formation of autophagic vacuoles and the sequestrations of both cytoplasmic and lysosomal enzymes. However, when cycloheximide was administered 1 h after leupeptin, the formation of autophagosomes and the sequestration of cytoplasmic enzymes were inhibited but the vacuolar uptake of acid phosphatase and cathepsin D continued to increase for several hours. When cycloheximide was injected 1 h after leupeptin, losses of lactic dehydrogenase and aldolase proteins were observed in autophagic vacuoles isolated 1 and 2 h later.
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PMID:Sequestration of cytoplasmic enzymes in an autophagic vacuole-lysosomal system induced by injection of leupeptin. 613 57

Twenty Thoroughbred 3 year old horses (10 stallions and 10 mares), trained and raced at the Warsaw Race-Course were studied from March through November. Blood was taken approximately every 8 weeks to determine the activities of aspartate and alanine transaminases, acid and alkaline phosphatases and aldolase. It was observed that the activities of aspartate aminotransferase and alkaline phosphatase reached their maxima in July and alanine transaminase in May. The activities of acid phosphatase and aldolase showed their minima in July. Comparing these data with the literature it was noted that the changes observed are mainly seasonally-dependent; but, training had some influence on the activity of the enzymes involved in energy metabolism.
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PMID:Seasonal enzyme activity changes in two aminotransferases AspAT and AlAT, acid and alkaline phosphatases and aldolase in the serum of Thoroughbred horses during a racing season. 653 19

Oral administration of lantana leaf powder to guinea pigs caused an increase in the hepatic postmitochondrial fraction:homogenate ratios of activities of lysosomal enzymes--acid phosphatase, cathepsin B and DNase II. Enzyme activities of glucokinase, aldolase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase were elevated whereas activity of glutathione-S-transferase decreased. Alterations in the activities of lysosomal and cytosol enzymes appear to constitute an important biochemical lesion in the pathogenesis of guinea pig liver in lantana toxicity.
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PMID:Effect of lantana toxicity on lysosomal and cytosol enzymes in guinea pig liver. 683 12

In rabbits, the right hind limb was immobilized by means of plaster cast for 1, 2, 4 or 6 weeks and the activities of some metabolic enzymes: GOT, GPT, LDH, aldolase and acid phosphatase (in part of lysosomal origin), were examined in the slow m. soleus, and in the fast m. gastrocnemius. The former muscle is known to have mainly an oxidative, while the latter mainly a glycolytic type of metabolism. The activities of enzymes highly involved in the metabolism of the muscle diminished for a certain time during atrophy, then a relative rise occurred. Acid phosphatase activity likewise decreased after an initial relative increase. Reduction of enzymatic activities is explained by the activation of proteolytic enzymes, on the basis of measurements performed in these experiments and of results published by others. The decrease of enzymatic activity was more marked in the muscle which in normal state exhibits higher activity than in the other type of muscle studied. Thus, in the gastrocnemius a high rate of degradation of glycolytic enzymes was observed, while in the soleus degradation of oxidative enzymes prevailed. This phenomenon leads to the dedifferentiation of the muscle cell during immobilization.
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PMID:Experimental studies on hypokinesis of skeletal muscle with different functions. VI. 716 67

The authors performed a comparative biochemical study of some enzymes of lysosomic origin (hyaluronidase, N-acetyl-beta-D-glucosaminidase, beta-glucosidase, beta-galatosidase and acid phosphatase), of the state of enzyme substrate system N-acetylneuraminic acid---aldolase of neuramic acid and of the activity of lactatedehydrogenase (soluble in cytosol and bound on mitochodria) in the liver, lungs and blood serum of rats at various regimens of the inhalation action of CCl4. On the basis of results obtained they determined the biological importance of the change of activity of enzymes differently localized in cells at the adaptation of an organisme to the noxious action of CCl4.
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PMID:The influence of tetrachloromethane on subcellular structures of rat hepatocyte lysosomal and cytoplasmic enzymes of the liver, lungs and blood serum of rats during continuous and intermittent action of tetrachloromethane. 719 Sep 85

Homogenates of the posterior latissimus dorsi muscle, a phasic muscle, were fractionated by a one-step zonal centrifugation technique into four major organelle populations and cytoplasmic constituents. These were: (1) Plasma membrane fragments with a modal equilibrium density of 1.10 and containing 5'-nucleotidase, alkaline phosphodiesterase, p-nitrophenylphosphatase and acid phosphatase (beta-glycerophosphate was used as the substrate). (2) Sarcoplasmic reticular fragments which could be further subdivided into calcium transport vesicles, with a model equilibrium density of 1.16, that exhibited calcium uptake; K+-ATPase; leucyl-bet-naphthylamidase; acid phosphodiesterase; acid phosphatase (using cytidine monophosphate as the substrate); and sarcoplasmic reticular lysosomes, with a model equilibrium density of 1.18, possessing dipeptidyl-aminopeptidase II, cathepsin D, alpha-glucosidase, N-acetyl-beta-glucosaminidase, and NADH oxidase activity. (3) Mitochondria with a modal equilibrium density of 1.21. (4) Catalase-containing vesicles with a modal equilibrium density of 1.22; and cytoplasmic constituents (modal density of 1.25) with phosphorylase, pyruvate kinase, myosin-ATPase, aldolase, and protein and RNA content. The purity of these organelles was equal to or better than previous efforts, with a 30-fold purification achieved for 5'-nucleotidase and alkaline phosphodiesterase. These results lend support to the hypothesis that the sarcoplasmic reticulum of phasic muscle, in addition to its specialized role in excitation-contraction coupling, represents a multifunctional membrane system, and that, similar to the smooth endoplasmic reticulum of other cells, it includes some membrane-bound lysosomal enzymes and NADH oxidase.
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PMID:Isopycnic-zonal centrifugation of plasma membrane, sarcoplasmic reticular fragments, lysosomes, and cytoplasmic proteins from phasic skeletal muscle. 721 87

The intralysosomal localization of the enzymes that catalyse inactivation of rat liver fructose-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) to a form with antigenic activity was demonstrated. The inactivating enzymes like all other lysosomal markers tested except acid phosphatase, were readily solubilized by hypotonic shock. The inactivating enzyme activity was inhibited by PMSF, TPCK, TLCK and leupeptin, but not by pepstatin. On partial purification of the inactivating activity from the lysosomal fraction by DEAE-Sephadex (A-50) and Sephadex G-100 column chromatographies, it was copurified with lysosomal carboxypeptidase A and cathepsin B (EC 3.4.22.1). Studies on its substrate specificity and sensitivity to inhibitors indicated that cathepsin B and carboxypeptidase A are responsible for almost all the aldolase-inactivating activity in the lysosomal fraction.
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PMID:Properties of fructose-1,6-bisphosphate aldolase inactivating enzymes in rat liver lysosomes. 726 Jan

the activities of eight enzymes were determined in the regenerating liver of rats after partial hepatectomy. For five enzymes, i.e., aldolase, lactate dehydrogenase, alanine transaminase, 5-nucleotidase, and acid phosphatase a progressive statistically significant increase in activities was obtained on days 10 and 20 of regeneration. This increase was not at the high level observed for parallel activities in fetal liver of rats on the 20th day of gestation. A possible interpretation of the process of liver regeneration is suggested.
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PMID:Enzyme activities in regenerating liver of rats. 740 87


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