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)

To evaluate the participation of proteins derived from mitochondrial genes in the adaptive response of skeletal muscle to increased contractile activity, we administered chloramphenicol (CAP; 200-1,000 mg.kg-1.day-1), an inhibitor of translation from mitochondrial ribosomes, to adult rabbits undergoing electrical stimulation of the tibialis anterior muscle of one hind limb. In unmedicated animals, 10 days of electrical stimulation increased maximum velocity (Vmax) of cytochrome oxidase and citrate synthase by 214 +/- 17 and 201 +/- 16% (P less than 0.01). In a dose-dependent manner, CAP abolished activity-induced increases in cytochrome oxidase Vmax, suggesting that augmented mitochondrial protein synthesis is necessary for the adaptive response of enzymes that require protein subunits encoded by mitochondrial genes. However, CAP failed to inhibit activity-induced changes in Vmax of enzymes derived exclusively from nuclear genes (citrate synthase and aldolase). CAP also failed to inhibit activity-induced increases in mRNA transcribed from the nuclear genes encoding beta-F1 ATPase or myoglobin, or from the mitochondrial genes encoding 12S rRNA, 16S rRNA, or cytochrome b. These latter findings suggest that mitochondrial translation products do not participate in pretranslational regulation of these nuclear or mitochondrial genes in response to changes in contractile activity of skeletal muscle.
Am J Physiol 1987 Dec
PMID:Effects of inhibition of mitochondrial protein synthesis in skeletal muscle. 289 13

Isoenzyme patterns of adult Malaysian Schistosoma, S. mekongi and S. japonicum strains were analysed by isoelectric focusing (IEF) in polyacrylamide gel. Enzyme patterns obtained from Malaysian Schistosoma homogenates differed from those of S. mekongi and S. japonicum strains. Malaysian Schistosoma was found to differ from S. japonicum by 8 enzymes, namely phosphoglucomutase, phosphoglucoisomerase, malate dehydrogenase, acid phosphatase, hydroxy-butyrate dehydrogenase, hexokinase and alkaline phosphatase, and from S. mekongi by phosphoglucomutase, malate dehydrogenase, aldolase and alkaline phosphatase. These results and the distinct biology of the parasite suggest that Malaysian Schistosoma is a new species in the S. japonicum complex.
Southeast Asian J Trop Med Public Health 1985 Dec
PMID:Isoenzyme analyses of Malaysian Schistosoma, S. mekongi and S. japonicum by isoelectric focusing in polyacrylamide gel. 294 Jun 88

Mucinase enzymes were isolated and partially purified from the culture fluid of Vibrio cholerae grown in proteose peptone-colostrum medium. The mucinase complex contained neuraminidase, endo-beta-N-acetylhexosaminidase, nicotinamide-adenine-dinucleotidase and proteinases. Traces of phospholipase activity were detected but the complex lacked aldolase activity.
J Med Microbiol 1986 Dec
PMID:Studies on the Vibrio cholerae mucinase complex. I. Enzymic activities associated with the complex. 302 45

Enzymes of the glycolytic pathway as well as some ancillary enzymes were studied in normal red cells parasitized with Plasmodium falciparum in culture at varying parasitemias as well as in isolated parasites. The levels of all enzymes except diphosphoglycerate mutase, glucose-6-phosphate dehydrogenase, and adenylate kinase were elevated. Extreme elevations of hexokinase, aldolase, enolase, pyruvate kinase, and adenosine deaminase concentrations were noted. In most cases, electrophoretically distinct bands of enzyme activity were also seen. These findings partly explain the previously noted 50- to 100-fold increase in glucose consumption of infected red cells and suggest that further knowledge of these parasite enzymes and their genetic basis may aid both in designing new chemotherapy and in understanding the evolution of these parasites.
Blood 1988 Dec
PMID:The enzymes of the glycolytic pathway in erythrocytes infected with Plasmodium falciparum malaria parasites. 305 30

Serum aldolase B levels were determined in patients with malignant tumors using a radioimmunoassay method. Thirty-one of 52 patients with malignant tumors had decreased serum aldolase B levels of less than 20 ng/ml, whereas almost all of the normal subjects and the patients with liver diseases and other benign diseases showed serum aldolase B levels of more than 20 ng/ml. The decreased aldolase B levels observed in cancer patients were unrelated to the clinical stage of their disease. The decrease of aldolase B correlated well with the decrease of fructose-1-phosphate (F1P)-aldolase activity, but not with fructose-1,6-diphosphate (FDP)-aldolase activity in the sera of cancer patients. Mixing experiments did not identify an inhibitor of aldolase B in sera of cancer patients. Furthermore, recovery of serum aldolase B levels after successful surgical resection in cancer patients suggested that the low levels of aldolase B in sera of cancer patients was not of genetic origin. The mechanism responsible for the decrease of aldolase B in sera of cancer patients is unclear.
Cancer 1988 Dec 15
PMID:Decreased serum aldolase B levels in patients with malignant tumors. 319 54

Srivastava and Bernhard [Srivastava, D. K. & Bernhard, S. A. (1986) Science 234, 1081-1086] have proposed that glycolytic enzymes form multienzyme complexes for the direct transfer of metabolites from the producing enzyme to the utilizing one. We have reinvestigated the evidence for direct transfer of NADH between its complexes with alpha-glycerol-3-phosphate dehydrogenase (GPDH; EC 1.1.1.8) and L-lactate dehydrogenase (LDH; EC 1.1.1.27). The results reveal the following. (i) Proper treatment of the kinetics of and equilibrium data for the transfer of NADH between GPDH and LDH indicates that NADH transfer proceeds by a free-diffusion mechanism and not by direct transfer through a ternary complex. (ii) The koff for NADH from its GPDH complex is 60 sec-1 rather than 9.4 sec-1 in Tris.HCl buffer (pH 7.4) at 25 degrees C. With this value one can explain kcat = 50 sec-1 for LDH-catalyzed hydrogenation of pyruvate with GPDH-bound NADH as coenzyme. (iii) Steady-state kinetics show that LDH inhibits the GPDH-catalyzed reaction simply by reducing the concentration of free NADH. Similarly, aldolase inhibits the GPDH-catalyzed reduction of dihydroxyacetone phosphate to glycerol-3-phosphate by binding to the substrate. The proposed direct transfer of NADH between GPDH and LDH is therefore mainly based on a misinterpretation of the experimental data.
Proc Natl Acad Sci U S A 1988 Dec
PMID:Reexamination of the kinetics of the transfer of NADH between its complexes with glycerol-3-phosphate dehydrogenase and with lactate dehydrogenase. 319 95

Binding of the fluorescent Ca2+ indicator dye fura-2 by intracellular constituents has been investigated by steady-state optical measurements. Fura-2's (a) fluorescence intensity, (b) fluorescence emission anisotropy, (c) fluorescence emission spectrum, and (d) absorbance spectra were measured in glass capillary tubes containing solutions of purified myoplasmic proteins; properties b and c were also measured in frog skeletal muscle fibers microinjected with fura-2. The results indicate that more than half, and possibly as much as 85%, of fura-2 molecules in myoplasm are in a protein-bound form, and that the binding changes many properties of the dye. For example, in vitro characterization of the Ca2+-dye reaction indicates that when fura-2 is bound to aldolase (a large and abundant myoplasmic protein), the dissociation constant of the dye for Ca2+ is three- to fourfold larger than that measured in the absence of protein. The problems raised by intracellular binding of fura-2 to cytoplasmic proteins may well apply to cells other than skeletal muscle fibers.
Biophys J 1988 Dec
PMID:Myoplasmic binding of fura-2 investigated by steady-state fluorescence and absorbance measurements. 326 79

The glycolytic enzymes of Trypanosomatids are compartmentalized within peroxisome-like microbodies called glycosomes. Fructose bisphosphate aldolase is synthesized on free polysomes and imported into glycosomes within 5 min. Peptide mapping reveals no primary structural differences between the in vivo-synthesized protein and that made in vitro from a synthetic template. However, native aldolase from glycosomes is partially protease resistant, whereas the in vitro translation product is not. Pulse-chase results indicate that aldolase in bloodstream trypanosomes has a much longer half-life than in the procyclic tsetse fly form.
J Cell Biol 1987 Dec
PMID:Import of fructose bisphosphate aldolase into the glycosomes of Trypanosoma brucei. 332 52

Activity of glucose-6-phosphate dehydrogenase (I), fructose diphosphate aldolase (II) and succinate dehydrogenase (III) and content of pyruvate (IV) in the mycelium of the oleandomycin-producing organism were studied during increased intensity of the antibiotic synthesis. The increase in the intensity of the antibiotic synthesis was induced by exposure of the spores to a surface active substance, twin-21. After the exposure a rise in the activity of all the three enzymes in the phase of the culture intensive growth was observed. During the antibiotic intensive production the cultures with increased antibiotic production levels were characterized by significantly higher activity of I as compared to the control while the activity levels of II and III were approximately the same. It was shown that concentration of IV in the mycelium during the antibiotic intensive biosynthesis decreased and the decrease was more pronounced after exposure to twin-21.
Antibiot Med Biotekhnol 1987 Dec
PMID:[Effect of surface-active substances on carbohydrate metabolism in the producer of oleandomycin]. 332 23

Fructose-1,6-bisphosphate and triosephosphates have been separated by high performance liquid chromatography utilizing a SynChropack AX anion exchange column with 50-200 mM KH2PO4, pH 2.5-4.6 as mobile phase. The best resolution for each compound was reached in a system of 150 mM KH2PO4, pH 2.5. If radioactive fructose-1,6-bisphosphate as initial substrate was enzymatically converted in triosephosphates, the recoveries of metabolites after the precipitation and chromatographic procedures were higher than 95%. The concentration of radioactive 3-phosphoglycerate measured by liquid scintillation shows a good correlation (correlation coefficient: 0.997) with the spectrophotometrically determined concentration of NADH, which is formed from [U-14C]fructose-1,6-bisphosphate in equimolar concentration with 3-phosphoglycerate in aldolase and glyceraldehyde-3-phosphate dehydrogenase system. The method developed was applied to detect the inhibitory effect of triosephosphate isomerase on aldolase activity which takes place due to the heterologous complex formation.
J Biochem Biophys Methods 1986 Dec
PMID:Quantitative determination of triosephosphates during enzymatic reaction by high performance liquid chromatography: effect of isomerase on aldolase activity. 355 36


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