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:2.7.1.1 (hexokinase)
5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Freshly isolated rabbit proximal tubules (PT), confluent primary rabbit proximal tubule cultures (PTC) and LLC-PK1 cells were characterised. Brushborder enzyme activities were lower in PTC than in LLC-PK1: ratios were 0.026 for alkaline phosphatase (AP), 0.458 for alanine aminopeptidase (AAP) and 0.514 for gamma-glutamyl transpeptidase (GGT). PT/PTC ratios were 79.7 for AP, 7.96 for AAP and 3.45 for GGT. Specific activities of hexokinase (HK) and lactate dehydrogenase (LDH) were high in cultured cells as compared to PT: PT/PTC ratios were 0.063 and 0.033, while PTC/LLC-PK1 ratios were 0.406 and 1.19 for HK and LDH respectively. PTC/LLC-PK1 ratios were 2.21 for Na/K ATPase, 2.07 for succinate dehydrogenase, 1.12 for cathepsin B, 0.607 for N-acetyl-beta-D-glucosaminidase and 8.98 for glutathione-S-transferase. Adenylate cyclase response to parathormone (PTH), was similar in PTC and PT, but stimulated/basal ratios were higher in PT than in PTC. LLC-PK1 cells were stimulated by thyrocalcitonin (SCT), arginin-vasopressin (AVP) and PTH; stimulated/basal ratios ranked AVP greater than PTH greater than SCT. Differences between both types of cultures affect the choice of in vitro model for nephrotoxicity studies.
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PMID:Adenylate cyclase responses and biochemical characterization of primary rabbit proximal tubular cell cultures and LLC-PK1 cells. 228 70

A fast and reliable two-step method has been established for the chemical synthesis of 6-thioguanosine 5'-monophosphate, 6-thioguanosine 5'-diphosphate and 6-thioguanosine 5'-triphosphate starting from the ribonucleoside. In the first step, 6-thioguanosine dissolved in triethyl phosphate, at high yield reacts with phosphorus oxide trichloride to 6-thioguanosine 5'-monophosphate which is purified by anion-exchange chromatography on DEAE-Sephadex using a step gradient of hydrochloric acid. In the second step, 6-thioguanosine 5'-monophosphate dissolved in water, reacts with phosphoric acid in the presence of pyridine/dicyclohexyl carbodiimide and is converted to 6-thioguanosine 5'-diphosphate and 6-thioguanosine 5'-triphosphate which are separated from each other and from the 6-thioguanosine 5'-monophosphate by anion-exchange chromatography on DEAE-Sephadex using a gradient of ammonium bicarbonate. Material from each step of the preparation procedure is separated by reversed-phase HPLC chromatography and analyzed for its free ribonucleoside content, 5'-monophosphate, 5'-diphosphate, 5'-triphosphate and small amounts of unidentified phosphorylated compounds. The purity of the final preparations and the identity of each 6-thioguanosine 5'-phosphate are proven by highly specific enzymatic peak-shifting/HPLC analyses using alkaline phosphatase, 5'-nucleotidase, pyruvate kinase, nucleoside diphosphate kinase and combined hexokinase/glucose 6-phosphate dehydrogenase.
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PMID:The quantitative determination of metabolites of 6-mercaptopurine in biological materials. VII. Chemical synthesis by phosphorylation of 6-thioguanosine 5'-monophosphate, 5'-diphosphate and 5'-triphosphate, and their purification and identification by reversed-phase/ion-pair high-performance liquid chromatography and by various enzymatic assays. 230 58

Procedures for the isolation and enrichment of cell populations from suspensions of rat kidney cortical cells were developed. Using Percoll density-gradient centrifugation, two populations of cells were obtained; marker enzymes [alkaline phosphatase and gamma-glutamyltransferase for proximal tubular (PT) cells and hexokinase for distal tubular (DT) cells] and functional responses (stimulation of PT cell oxygen consumption by succinate and inhibition of DT cell oxygen consumption by amiloride) were then employed to identify and assess the purity of the two fractions. The PT cell fraction was estimated to contain 97% PT cells and the DT cell fraction was estimated to contain 88% DT cells. Staining with toluidine blue and light microscopy showed that PT cells contained a brush border, were larger than DT cells, and had more intensely staining nuclei than DT cells. To demonstrate the usefulness of these cell preparations in the study of biochemical mechanisms of renal cell injury, time- and concentration-dependent effects of the PT cell-specific nephrotoxin cephaloridine (CPH) on PT and DT cell trypan blue exclusion were examined. CPH was toxic in PT cells but not in DT cells; viability of PT cells incubated with 0.1 or 1 mM CPH for 2 h was 57 or 34%, respectively, compared to 81% for control cells; viability of DT cells incubated with 0.1 or 1 mM CPH for 2 h was 74 or 71%, respectively, compared to 74% for control cells. This method thus provides highly enriched preparations of freshly isolated PT and DT cells that retain their unique properties and are suitable for studies of biochemical mechanisms of chemical toxicity and nephron heterogeneity.
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PMID:Isolation of two distinct populations of cells from rat kidney cortex and their use in the study of chemical-induced toxicity. 269 74

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.
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PMID:Isoenzyme analyses of Malaysian Schistosoma, S. mekongi and S. japonicum by isoelectric focusing in polyacrylamide gel. 294 Jun 88

Ancylostoma ceylanicum infection in golden hamsters (Mesocricetus auratus) caused marked biochemical and histopathological derangements. Jejunum, the primary site of infection, showed pronounced alterations compared with liver. Though the biochemical composition of jejunum was not significantly altered, activities of a few lysosomal enzymes were enhanced during hookworm infection. Marked damage to mitochondrial and microsomal membranes was reflected in changes in the activities of the marker enzymes from jejunal tissue. Lipid content, especially phospholipids and neutral lipids of hepatic tissue, exhibited marked elevation. Levels of hexokinase, phosphofructokinase, and lactate dehydrogenase were enhanced in jejunal as well as hepatic tissues, indicating activation of the glycolytic machinery during hookworm infection. A decrease in the levels of mucosal disaccharidases indicated damage to intestinal brush border membranes. However, alkaline phosphatase activity was increased in intestinal mucosa during the infection. Light microscopic examination of jejunal tissue revealed peeling off of the upper epithelial layer, activation of the goblet cells, and thickening of muscularis mucosa. However, hepatic tissue did not show gross alterations, except for slight necrosis in the centrilobular region.
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PMID:Biochemical and histopathological alterations in golden hamster during infection with Ancylostoma ceylanicum. 339 68

Alterations in the activities of some enzymes in a freshwater catfish, Heteropneustes fossilis, have been examined in liver, kidney, intestine, ovary, gills, and muscles after exposure to 0.26 mg/liter of cadmium for 15, 30, and 60 days. The fish were hyperglycemic and hyperlactemic after 15 and 30 days of exposure. The liver and muscle glycogen content was depleted in the first two periods of exposure. In contrast, 60 days of cadmium treatment increased the glycogen content of the two tissues. Liver lactic acid level was elevated after 15 days. Muscle lactic acid content fell significantly after 15 and 60 days of exposure, but it was elevated after 30 days. Acid phosphatase activity was inhibited in liver, ovary, and gills but the enzyme activity increased in kidney and intestine. The activity of alkaline phosphatase decreased in liver, kidney, and intestine but elevation was recorded in ovary and muscles. In all three exposure periods, hexokinase activity of kidney and ovary was inhibited but the enzyme activity increased in intestine. Hexokinase showed elevation in liver, gills, and muscle after 15 and 30 days of exposure and inhibition after 60 days of exposure. The activity of xanthine oxidase decreased in liver and muscles and elevated in the rest of the tissues. Glutamate dehydrogenase fell significantly in intestine, ovary, and gills. In liver, kidney, and muscles the enzyme activity was elevated. Liver, intestine, gills, and muscles showed elevation in aminoacid oxidase activity. However, the enzyme activity was inhibited in kidney and in ovary.
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PMID:In vivo effects of cadmium on some enzyme activities in tissues of the freshwater catfish, Heteropneustes fossilis. 383 54

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1mum-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.
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PMID:The inhibition of enzymes by beryllium. 428 87

A study was made of the enzyme content of the isolated cell walls and of a plasma-membrane preparation obtained by centrifugation after enzymic digestion of the cell walls of baker's yeast. The isolated cell walls showed no hexokinase, alkaline phosphatase, esterase or NADH oxidase activity. It was concluded that these enzymes exist only in the interior of the cell. Further, only a negligible activity of deamidase was detectable in the cell walls. Noticeable amounts of saccharase, phosphatases hydrolysing p-nitrophenyl phosphate, ATP, ADP, thiamin pyrophosphate and PP(i), with optimum activity at pH3-4, and an activity of Mg(2+)-dependent adenosine triphosphatase at neutral pH, were found in the isolated cell walls. During enzymic digestion, the other activities appearing in the cell walls were mostly released into the medium, but the bulk of the Mg(2+)-dependent adenosine triphosphatase remained in the plasma-membrane preparation. Accordingly, it may be assumed that the enzymes released into the medium during digestion are located in the cell wall outside the plasma membrane, whereas the Mg(2+)-dependent adenosine triphosphatase is an enzyme of the plasma membrane. This enzyme differs from the phosphatases with pH optima in the range pH3-4 with regard to location, pH optimum, substrate specificity and different requirement of activators.
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PMID:The enzymic composition of the isolated cell wall and plasma membrane of baker's yeast. 431 24

In accord with previous studies, (I)n . (C)n, a potent inhibitor of the cell-free protein-synthesizing system of interferon-treated L cells, stimulates incorporation of 32P from [gamma-32P]ATP into the 67,000-dalton protein, P1. The double-stranded RNA (I)n . (br5C)n, which is inactive as an inhibitory of protein synthesis, does not stimulate phosphorylation of P1 under conditions approximating those of protein synthesis. However, we have found conditions under which (I)n . (br5C)n is approximately as effective as (I)n . (C)n in stimulating incorporation of label from [gamma-32P]ATP into 67,000-dalton protein. Upon transfer of labeled P1 from these conditions to those compatible with protein synthesis, there is a time-dependent decrease in label in the 67,000-dalton protein. This decrease is more rapid in the presence of (I)n . (br5C)n than in the presence of (I)n . (C)n. This differential decrease is also observed when 32P-labeled extracts are diluted into buffer containing 10 mM ATP, hexokinase and 1 and M glucose, or Escherichia coli alkaline phosphatase. A partial proteolytic digest of P1 labeled in the absence of double-stranded RNA or in the presence of (I)n . (C)n or (I)n . (br5C)n gives rise to similar peptide patterns. These results suggest that dephosphorylation as well as phosphorylation determines the net incorporation of 32P into P1. Moreover, these results suggest the existence of a phosphatase activity that may be inhibited more strongly by (I)n . (C)n than by (I)n . (br5C)n.
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PMID:Double-stranded RNA inhibits a phosphoprotein phosphatase present in interferon-treated cells. 624 37

Four aspects of the behavior of 3-deoxy-3-fluoro-D-glucose (D-3FDG) were studied. The distribution of label in rat tissues after intravenous administration of [18F]D-3FDG was compared with that seen with labeled 3-deoxy-3-fluoro-L-glucose (L-3FDG). Results were consistent with a larger volume of distribution for the physiological D-isomer coupled with some degree of reabsorption by the kidneys. L-3FDG, but not its D-isomer, was excluded from the brain. D-3FDG competitively inhibited uptake of glucose by isolated perfused rat hearts. The inhibition constant was 12.8 +/- 1.6 mM compared with 6.1 +/- 1.1 mM for 3-O-methyl-D-glucose. Residue curves obtained after bolus administration of [18F]D-3FDG to isolated hearts indicated phosphorylation of the tracer at a lower rate than for 2-deoxy-2-fluoro-D-glucose but with subsequent dephosphorylation at a faster rate. Chromatographic analysis of 18F remaining in tissues after administration of [18F]D-3FDG revealed in addition to free D-3FDG three other peaks. These disappeared after treatment with alkaline phosphatase and were thus assigned as phosphates. The principal metabolite had the same retention time as D-3FDG-6-phosphate prepared with hexokinase. No phosphorylated metabolites were detected in blood. D-3FDG labeled with 18F may be a useful tracer in studies of glucose transport and metabolism.
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PMID:Validation of 3-deoxy-3-fluoro-D-glucose as a glucose transport analogue in rat heart. 649 56


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