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:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Protein turnover in the extreme bacterial thermophile Thermus aquaticus was examined in exponential cultures at 75 degrees C. The relative amount of [3H]leucine incorporated into trichloroacetic acid-insoluble material was stable in pulse-chase experiments assayed over 2.5 h. The trichloroacetic acid-insoluble radioactive leucine was stable upon the addition of chloramphenicol, which blocks protein synthesis in T. aquaticus. The specific activity of a phosphate-repressible alkaline phosphatase, investigated in the presence of chloramphenicol, did not decrease. The addition of excess orthophosphate to cultures derepressed for the alkaline phosphatase did not show a marked effect on the specific activity over a 2-h period. On the basis of these four experiments, it does not appear that a high protein turnover rate is essential for the thermophily of T. aquaticus at 75 degrees C.
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PMID:Protein turnover in the extreme thermophile Thermus aquaticus. 50 May 61

The nucleoprotein of the WSN strain of influenza was found to be phosphorylated in vitro. The phosphate-protein bond was stable to hot trichloroacetic acid, RNase, DNase, succinic acid, and succinic acid-hydroxylamine, but sensitive to hydrolysis by bacterial alkaline phosphatase. This suggested that the nucleoprotein is in the form of a phosphomonoester. Acid hydrolysis of the isolated nucleoprotein followed by thin-layer electrophoresis identified the phosphorylated amino acid residue as phosphoserine.
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PMID:Phosphorylated protein component present in influenza virions. 90 30

The supra- and suboesophageal ganglia of the American cockroach contain material which catalyses the alkaline hydrolysis (pH 9.5) of 5-bromo-4-chloro-3-indolyl phosphate in the presence of Nitro blue tetrazolium. Histochemical studies on unfixed cryostat sections indicate that this type of alkaline phosphatase is restricted to discrete regions in the cockroach brain. Highest enzyme activity is encountered in the mushroom bodies, central body, antennal glomeruli and specific parts of some distinct neural connections including the optic nerve, antennal nerve, circumoesophageal connectives and nerves leaving the suboesophageal ganglion. Tissue fixation by use of formaldehyde-type fixatives, as well as routine paraffin-embedding, completely destroy all histochemically detectable enzyme activity. Native polyacrylamide gradient electrophoresis suggests that the alkaline phosphatase activity is present as multiple isozymic forms, which show up in the 120-130 kD range of standard proteins. Enzyme activity becomes undetectable after fixation (trichloroacetic acid, formaldehyde containing fixatives) of electrophoretically separated native proteins, as well as after electrophoresis in denaturing conditions (SDS and beta-mercapto-ethanol, boiling). However, the enzyme activity remains virtually unaffected after storage of the sample for prolonged periods at -20 to -80 degrees C.
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PMID:Alkaline phosphatase activity in the brain of the American cockroach Periplaneta americana L. 207 11

We have developed an enzyme immunoassay (ELISA) for the quantification of the schistosome circulating cathodic antigen (CCA), a glycoprotein associated with the syncitium lining the gut of the parasite. A mouse monoclonal antibody of IgG3 isotype was used as coating (antigen-capture) antibody, while a biotinylated mouse monoclonal IgM was used as second (antigen-detecting) antibody. Streptavidin-alkaline phosphatase was used as enzyme label. The lower detection limit of the assay was 1.0 ng of the trichloroacetic acid soluble fraction of adult worm antigen (AWA-TCA) per ml, which corresponds to approximately 0.2 ng CCA per ml. The ELISA showed a linear range from 1.0 to 62.5 ng AWA-TCA per ml. Serum and urine samples of 16 individuals infected with Schistosoma mansoni (egg counts ranging from 5 to 4820 eggs per gram of faeces) were tested in the assay. Antigen titres ranged from less than 4-8192. This assay represents a considerable advantage in diagnosis of Schistosoma infections as it allows the detection and quantification of CCA in serum and urine in even lightly infected individuals.
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PMID:Detection of the schistosome circulating cathodic antigen by enzyme immunoassay using biotinylated monoclonal antibodies. 212 84

The purpose of the study was to investigate the effect of skeletal growth factor/insulinlike growth factor II and other growth factors known to be present in bone matrix on the proliferation and differentiation of human bone cells. Cells were isolated by collagenase digestion from femoral heads obtained during hip replacement operations. Cells were cultured in DMEM medium with 10% calf serum. Third to fifth passage cells were plated in multiwell plates and the medium changed to low serum (0.1%) for 2 days. The medium was changed to serum-free medium prior to addition of growth factors. Cell proliferation was measured by the incorporation of [3H]thymidine into DNA and by the percentage of cells that incorporate bromodeoxyuridine. Protein synthesis was measured by the incorporation of [3H]proline into trichloroacetic acid-precipitable material. Skeletal growth factor/insulinlike growth factor II and insulinlike growth factor I stimulated cell proliferation and protein synthesis in a dose-dependent manner. Alkaline phosphatase-specific activity was not increased by these factors. Transforming growth factor beta 1 did not affect cell proliferation but stimulated protein synthesis and increased the specific activity of alkaline phosphatase. Fibroblast growth factor did not affect any of the cell parameters. These studies suggest that skeletal growth factor/insulinlike growth factor II, insulinlike growth factor I, and transforming growth factor beta 1 may play a role in the local control of the proliferation and differentiation of human osteoblasts.
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PMID:Skeletal growth factor and other growth factors known to be present in bone matrix stimulate proliferation and protein synthesis in human bone cells. 215 9

Male Sprague-Dawley rats were treated with either dichloroacetic acid (DCA) or trichloroacetic acid (TCA) in the drinking water at levels of 0, 50, 500 and 5000 ppm for a period of 90 days to determine the toxicities associated with subchronic exposure. All animals were sacrificed and examined for gross and histopathologic lesions, serochemical changes, immune dysfunction, hepatic peroxisomal and mixed function oxidase enzyme induction and organ-body weight changes. Animals treated with DCA had decreased body weight gains (500 and 5000 ppm) and decreased total serum protein (all doses). Rats given either TCA (5000 ppm) or DCA (500 or 5000 ppm) had increased liver and kidney organ to body weight ratios. Rats offered DCA had significantly elevated alkaline phosphatase (500 and 5000 ppm) and alanine-amino transferase (5000 ppm). No consistent immunotoxicity was observed in animals exposed to either compound. Rats treated with 5000 ppm TCA or DCA had significantly increased hepatic peroxisomal beta-oxidation activity. These data, along with histopathologic changes, suggest that TCA and DCA produce substantial systemic organ toxicity to the liver and kidney during a 90-day subchronic exposure, although only at doses greater than those expected to occur in the environment.
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PMID:Subchronic 90 day toxicity of dichloroacetic and trichloroacetic acid in rats. 221 34

We report the development of a time-resolved immunofluorometric assay (TR-IFMA) for the quantitative determination of the schistosome circulating anodic antigen (CAA). A mouse monoclonal antibody (line 120-1B10-A), recognizing a repetitive epitope on CAA, was used as both antigen-capture antibody and as Europium-labelled antigen-detecting antibody. The lower detection limit of the assay was 20 pg of trichloroacetic acid soluble fraction of adult worm antigen (AWA-TCA) per ml, with a nearly linear measuring range from 20 pg to 130 ng AWA-TCA per ml. The TR-IFMA was compared with an enzyme-linked immunosorbent assay (ELISA), in which the same monoclonal antibody was used as antigen-capture antibody and as alkaline phosphatase-conjugated antibody. The lower detection limit of the TR-IFMA was tenfold lower than that of the ELISA, while the linear range of the TR-IFMA exceeded that of the ELISA one hundred-fold. Serum samples of 80 Burundese individuals infected with Schistosoma mansoni (egg counts ranging from 4 to 2583 eggs per gram of faeces) were tested in both assays. Antigen concentrations in serum of individuals infected with S. mansoni ranged from 0-500 ng AWA-TCA per ml. The correlation between antigen levels measured by TR-IFMA and ELISA was good: Spearman's p = 0.92. Whereas in the ELISA the samples had to be titrated, the wide linear range of the TR-IFMA allowed the assay to be performed at a single serum dilution, at which an exact estimation of the antigen concentration was possible.
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PMID:Time-resolved immunofluorometric assay (TR-IFMA) for the detection of the schistosome circulating anodic antigen. 251 32

In culture, 1-p-bromotetramisole (pBTM), a specific inhibitor of alkaline phosphatase, significantly inhibited the formation of trichloroacetic acid (TCA)-insoluble [32P]-phosphate from inorganic [32P]-phosphate in the proliferating non-mineralizing second (M2) maxillary molar germs but had no effect in the actively mineralizing first (M1) germs. Addition of 10(-5) M inorganic pyrophosphate in the culture medium with a [32P]-phosphate label increased the inhibition of the formation of TCA-insoluble [32P]-phosphate in the M2. pBTM almost completely inhibited the formation of TCA-insoluble [32P]-phosphate from inorganic [32P]-pyrophosphate in the non-mineralizing M2. In the actively mineralizing M1, the compound significantly inhibited but did not abolish the formation of TCA-insoluble phosphate. These results confirm earlier biochemical findings that alkaline phosphatase possesses a pyrophosphatase activity probably related to the turnover of phosphorylated macromolecules necessary for cell differentiation and proliferation.
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PMID:Effect of alkaline-phosphatase inhibition by 1-p-bromotetramisole on the formation of trichloroacetic acid-[32P]-insoluble phosphate from inorganic [32P]-phosphate and [32P]-pyrophosphate in non-mineralizing and mineralizing hamster molar tooth-germs in vitro. 282 59

Murine T-lymphomas and Thy-1- mutants were labeled overnight with [3H]ethanolamine to detect proteins which possess a glycophospholipid anchor. When labeled cells were treated with 10% trichloroacetic acid and then analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography, both Thy-1 and a second intensely labeled protein (46 kDa) were observed. The presence of the radiolabeled 46-kDa protein in wild type and class E Thy-1 negative cells (cells in which Thy-1 is synthesized but cannot be labeled with [3H]ethanolamine) suggested incorporation into a distinct moiety. Labeling of the 46-kDa protein with [3H]ethanolamine is rapidly inhibited by cycloheximide. Further characterization of the 46-kDa protein by subcellular fractionation and Triton X-114 partitioning indicated that the protein is located in the cytosol. The protein is basic and does not bind to either concanavalin A or wheat germ agglutinin. Labeling of a 46-kDa protein has also been demonstrated in Chinese hamster ovary, COS, rat myeloma, cloned human T-lymphocytes, and HeLa cells. Pronase digestion of the [3H]ethanolamine-labeled 46-kDa protein of wild type lymphoma cells generated a nonbasic and polar labeled fragment which is labile to strong acid and base ([3H]ethanolamine is liberated), insensitive to periodate oxidation and alkaline phosphatase, and does not bind to concanavalin A or wheat germ agglutinin. Judging from methylation studies, the labeled ethanolamine residue does not contain a free amino group. Based on these results, we report a novel post-translational modification of selected protein(s) by the covalent addition of [3H]ethanolamine.
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PMID:Extensive labeling with [3H]ethanolamine of a hydrophilic protein of animal cells. 337 24

Endogenous oligonucleotides were found in trichloroacetic acid extracts of hamster lung fibroblasts and Tetrahymena cells. Peaks of radioactivity that eluted with retention times similar to oligonucleotide markers (5- to 50-mer) were found by HPLC in cells labeled briefly with 32Pi. Only minute amounts of UV-absorbing material were detected, consistent with a rapid turnover of phosphate groups. The 32P-labeled material also migrated as oligonucleotides on 20% polyacrylamide gels; it was not hydrolyzed by alkaline phosphatase but was digested by snake venom phosphodiesterase, S1 nuclease, and pancreatic RNase and was phosphorylated by T4 polynucleotide kinase. The 32P-labeled material isolated by HPLC was alkali labile and the hydrolyzate ran as nucleotides on paper chromatography. It is concluded that the oligonucleotides are mainly oligoribonucleotides, but it is possible that oligodeoxynucleotides are also present.
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PMID:Oligonucleotides with rapid turnover of the phosphate groups occur endogenously in eukaryotic cells. 347 Jul 67


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