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)

A monoclonal antibody highly specific for (2'-5')adenylyladenosine oligonucleotides was used together with a 125I-labeled analog of this compound to detect and quantify phosphorylated and nonphosphorylated (2'-5')adenylyladenosine oligonucleotides in a variety of tissues and cells. These oligonucleotides were first assayed as a whole in perchloric acid extracts and then further individually characterized by HPLC analysis. Their sensitivity to alkaline phosphatase, snake venom phosphodiesterase, and T2 RNase was systematically checked. Nonphosphorylated (2'-5')adenylyladenosine oligonucleotides were found in mammalian tissues as well as in yeast and bacteria. In normal mouse brain, lung, heart, pancreas, spleen, kidney, and liver their concentrations ranged from 10 to 200 pmol/g wet weight, depending on tissue and strain. The oligonucleotides were mainly dimers, trimers, tetramers, and pentamers. In addition, phosphorylated (2'-5')adenylyladenosine oligonucleotides were shown in liver and kidney extracts.
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PMID:Immunological evidence for the in vivo occurrence of (2'-5')adenylyladenosine oligonucleotides in eukaryotes and prokaryotes. 642 31

The production of the bacteriocin ulceracin 378 by Corynebacterium ulcerans 378 was demonstrated during the growth of the organism on solid medium. Ulceracin 378 was not found in broth cultures and could not be extracted from the organisms by various solvents and salt solutions. Ulceracin 378 was not inducible by UV irradiation or mitomycin C treatments. Ulceracin 378 was active against all of the C. ulcerans strains tested and some related species, but it was not autoinhibitory. The active material was not phage related and was extracted from cultures grown on semisolid media composed of proteose peptone, Tween 80, Casamino Acids, glycerol, and sodium chloride. The yield was significantly reduced by either increasing the agar concentration or omitting Tween 80. Ulceracin 378 was resistant to DNase, RNase, phospholipases C and D, and alkaline phosphatase but was susceptible to proteolytic enzymes. This suggests that the active principle of ulceracin is protein in nature. Ulceracin 378 was partially purified by ammonium sulfate fractionation, dialysis, and chromatography on DEAE-cellulose.
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PMID:Production of a bacteriocin, ulceracin 378, by Corynebacterium ulcerans. 668 39

The pep4-3 mutation results in a 90-95% reduction in the levels of five vacuolar hydrolases in yeast, including proteinases A and B, carboxypeptidase Y, RNase(s) and the repressible alkaline phosphatase. The mutation is without effect on two secreted glycoproteins, on an enzyme of the vacuolar membrane, and on a proteinase located outside of the vacuole. Mutations at the PEP4 locus exhibit a dosage effect on the levels of some, but not all, of the enzymes whose expression requires the function of the gene.
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PMID:PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. 676 1

The effects of the sublethal concentration (0.012%) of Congo Red on Heteropneustes fossilis were studied after 30 days exposure. The RBC count haemoglobin (Hb)% and PCV decreased significantly. The total WBC count, MCV, MCH, and MCHC showed a significant increase. Serum calcium, serum cholesterol and blood urea nitrogen (BUN) were significantly elevated, whereas serum phosphorus was significantly reduced. The activities of serum alkaline phosphatase (AlPase), acid phosphatase (AcPase). RNase, GOT, GPT and amylase were also significantly elevated. The possible reasons for these changes are discussed.
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PMID:Haematological and biochemical characteristics of Heteropneustes fossilis under the stress of Congo Red (diphenyl disazo binaphthionic acid). 716 84

In this paper clinical similarities between sickle cell anemia patients and zinc deficient subjects, the latter as reported from the Middle East have been presented. Zinc levels in plasma, red cells, hair and neutrophils were decreased in our adult patients with SCA. The activities of certain zinc dependent enzymes such as plasma RNase, red cell carbonic anhydrase, leucocyte alkaline phosphatase, and deoxythymidine kinase activity in freshly synthesized collagen connective tissue were consistent with the concept that indeed zinc deficiency occurred in SCA patients. Zinc supplementation under controlled conditions showed that the SCA patients gained weight, their serum testosterone level increased and plasma ammonia level decreased. Finally, we also observed abnormal dark adaptation in some SCA patients which improved following zinc supplementation. Inasmuch as we have previously reported that the number of irreversible sickle cells decrease following zinc supplementation, we would like to suggest that zinc supplementation at earlier age may be benefical in preventing organ damage. In conclusion, zinc supplementation should be prescribed for patients with SCA, particularly if they show evidences for zinc deficiency.
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PMID:Zinc deficiency and effects of zinc supplementation on sickle cell anemia subjects. 729 Dec 6

DNases A1 and A2 have been purified to homogeneity from the hepatopancreas of Achatina fulica by a series of steps: acetate buffer extraction, ammonium sulfate precipitation and column chromatography on hydroxylapatite, phosphocellulose, Blue-Sepharose, and poly(A)-Sepharose. The purified enzymes are free of acidic phosphomonoesterase, phosphodiesterase, and RNase activities. They are slightly acidic glycoproteins with identical isoelectric point (6.90). On 0.1% SDS gel electrophoresis, DNase A2 had a molecular weight of 30,000 when dissolved in 1% SDS, but it had molecular weights of 17,500, 8,000, and 4,800 when dissolved in 1% SDS and 1% 2-mercaptoethanol. This was evidence that the enzyme consists of three different subunits joined by interchain disulfide bonds. DNases A1 and A2 are endonucleases working at acidic pH (3.5--6.0) and do not require divalent cations for their activities. The enzymes degrade poly(dA) 5 times faster and poly(dT) 3 times faster than heat-denatured DNA under optimal conditions but do not appreciably digest poly(dG) and poly(dC). We developed an analytical procedure for oligodeoxynucleotides by high-performance liquid chromatography. The phosphomonoester end group and the mode of degradation were examined by the method. The termini produced by the enzymes have 3'-phosphoryl and 5'-hydroxy end groups. The products of exhaustive hydrolysis contain di-, tri-, tetra-, and pentanucleotides and mononucleotide was barely detected. The hydrolyzing activities of DNases A1 and A2 are stimulated by polyamines such as spermine, spermidine, and putrescine, but are inhibited by synthetic polynucleotides and various drugs. Adenosine deaminase highly active on oligoadenylic acids was found in a crude DNase A fraction. The enzyme preparation has higher activity on 3'-adenylic acid than on 5'-adenylic acid. The first adenosine residue of oligoadenylic acids was deaminated considerably more rapidly than the second or succeeding ones.
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PMID:DNase A, a poly(dA) and poly(dT)-specific deoxyribonuclease from Achatina fulica. Purification and characterization. 733 15

Human epidermal growth factor (EGF) receptor mRNA was detected in cryopreserved tissue sections adherent to whole glass slides using in situ reverse transcriptase polymerase chain reaction. EGF receptor cDNA was synthesized in situ by reverse transcription using an EGF receptor-specific oligonucleotide primer. In situ polymerase chain reaction amplification in the presence of digoxigenin-11-dUTP and subsequent binding with an antidigoxigenin antibody conjugated to alkaline phosphatase allowed direct visualization. Because DNase, RNase, or proteinase K are not required, tissue integrity is maintained. EGF receptor mRNA is expressed in the basal layer of normal human skin epithelium and is significantly overexpressed in squamous cell tumor specimens, which is consistent with conventional analysis of EGF receptor expression. The assay is semiquantitative, quicker, more sensitive, and void of the nonspecific binding associated with in situ hybridization. In situ reverse transcriptase polymerase chain reaction using whole glass slides is ideally suited for detecting moderate to infrequently expressed transcripts in biopsy specimens.
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PMID:Detection of epidermal growth factor receptor mRNA in tissue sections from biopsy specimens using in situ polymerase chain reaction. 808 54

Alternative splicing of primary transcripts from the calcitonin/alpha calcitonin gene-related peptide (alpha CGRP) gene result in mature mRNAs encoding either calcitonin or alpha CGRP. We have produced sequence-specific, synthetic, biotinylated oligodeoxynucleotide probes that recognize calcitonin (exon 4), and alpha CGRP (exon 6) sequences as well as sequences common to both splice variants (exon 3) of this gene. Probes to exons 4 and 3 revealed strong cytoplasmic signals in rat parafollicular cells. In addition, a punctate nuclear signal was obtained with these probes. The alpha CGRP-specific (exon 6) probe resulted in weak cytoplasmic labelling of parafollicular cells, but produced a punctate nuclear labelling similar to that seen with the exon 4 and 3 probes. RNase digestion removed all the cytoplasmic and nuclear signals obtained with all probes. Hybridization with a thyroglobulin-specific probe failed to label parafollicular cells. A control (human enterovirus) probe yielded negative results, while a probe to rat somatostatin produced cytoplasmic labelling of a small subpopulation of parafollicular cells. Finally, a probe specific for beta CGRP mRNA labelled most, if not all, parafollicular cells. Fluorescent alkaline phosphatase development of in situ hybridizations could be combined with indirect immunofluorescence for CGRP. Analysis by fluorescence and confocal microscopy revealed that CGRP immunoreactive cells contained calcitonin, alpha CGRP and beta CGRP hybridization signals. Our results demonstrate that all three genes may be simultaneously expressed by thyroid parafollicular cells and show that synthetic biotinylated oligonucleotide probes can be used for highly precise localizations of primary transcripts in the nuclei of these cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Detection of primary and mature transcripts of calcitonin-gene-related peptide genes in rat parafollicular cells by light, fluorescence and confocal microscopy. 773 76

The antiamoebic effect of a crude drug formulation against Entamoeba histolytica was studied. In the traditional system of medicine in India, the formulation has been prescribed for intestinal disorders. It comprises of five medicinal herbs, namely, Boerhavia diffusa, Berberis aristata, Tinospora cordifolia, Terminalia chebula and Zingiber officinale. The dried and pulverized plants were extracted in ethanol together and individually. In vitro amoebicidal activity was studied to determine the minimal inhibitory concentration (MIC) values of all the constituent extracts as well as the whole formulation. The formulation had a MIC of 1000 micrograms/ml as compared with 10 micrograms/ml for metronidazole. In experimental caecal amoebiasis in rats the formulation had a curative rate of 89% with the average degree of infection (ADI) reduced to 0.4 in a group dosed with 500 mg/kg per day as compared with ADI of 3.8 for the sham-treated control group of rats. Metronidazole had a cure rate of 89% (ADI = 0.4) at a dose of 100 mg/kg per day and cured the infection completely (ADI = 0) when the dosage was doubled to 200 mg/kg per day. There were varying degrees of inhibition of the following enzyme activities of crude extracts of axenically cultured amoebae: DNase, RNase, aldolase, alkaline phosphatase, acid phosphatase, alpha-amylase and protease.
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PMID:The antiamoebic effect of a crude drug formulation of herbal extracts against Entamoeba histolytica in vitro and in vivo. 773 26

8-Oxo-7,8-dihydroguanosine triphosphate (8-oxo-dGTP) is formed from the oxidation of GTP in the nucleotide pools of cells during normal cellular metabolism and from exogenous sources. 8-Oxo-dGTP is a potent mutagenic substrate for DNA synthesis causing transversion mutations. In human cells this oxidized base is hydrolyzed to 8-oxo-7,8-dihydroguanosine monophosphate by 8-oxo-7,8-dihydroguanosine triphosphatase (8-oxo-dGTPase) to prevent the misincorporation of 8-oxo-dGTP into cellular DNA. In order to better understand specific human tissue and cell type responses to oxidative stress, we used colorimetric in situ hybridization, with an 8-oxo-dGTPase-specific antisense oligomer probe, to map, for the first time, the cellular distribution of 8-oxo-dGTPase mRNA in tissue sections of normal neonatal foreskin and adult human breast tissues. Paraffin embedded tissue sections were hybridized with a digoxigenin-labeled 39 base oligomer, antisense to 8-oxo-dGTPase cDNA. Hybridization of the probe to cells expressing the 8-oxo-dGTPase gene was visualized following immunodetection with an alkaline phosphatase-conjugated anti-digoxigenin antibody. Following color development, we were able to simultaneously identify tissue architecture and cell types with expression of the 8-oxo-dGTPase gene. There was no hybridization-specific color when sections were 'mock' hybridized, hybridized with a sense probe or treated with RNase. In skin dermis, fibroblasts express high levels of 8-oxo-dGTPAse mRNA. Within the epidermis, a gradient of expression was observed, from high to moderate levels in the replicating basal epithelial cells to undetectable in the non-mitotic suprabasal and granular epithelial cells. In the breast tissue, fibroblasts in the loosely connective tissue and myoepithelial cells expressed high levels of 8-oxo-dGTPase mRNA, while expression in the luminal epithelial cells was not detectable. Our data suggest that expression of 8-oxo-dGTP is heterogenous between cell types within an organ and may help to explain cell type-specific responses to oxidative stress, especially in replicating and potentially replicating cells with low levels of this protective protein.
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PMID:Cell type-specific expression of human 8-oxo-7,8-dihydroguanosine triphosphatase in normal breast and skin tissues in vivo. 785 59


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