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

A high-performance liquid chromatographic method to measure pseudouridine and other nucleosides in hydrolyzed unfractionated tRNA and in acid soluble tissue extracts is described. The method is based on the following steps: tRNA extraction and hydrolysis by a mixture of ribonuclease A, snake venom phosphodiesterase and bacterial alkaline phosphatase; nucleoside purification (in the case of acid soluble tissue extract) by affinity chromatography on a phenyl-boronate gel column; nucleoside separation and quantitation by high-performance liquid chromatography on an octadecylsilane column by a reversed polarity gradient elution. The procedure allows a very accurate quantitation of pseudouridine and some other nucleosides, and its sensitivity is such that only 20 micrograms of tRNA are required. The method has been utilized to compare the pseudouridine content of hydrolyzed tRNA extracted from normal and lymphomatous murine thymus, as well as the pseudouridine content in acid soluble extracts from the same tissues.
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PMID:Determination of pseudouridine in tRNA and in acid-soluble tissue extracts by high-performance liquid chromatography. 648 Jul 46

ADP-ribosyl protein lyase, formerly termed ADP-ribosyl histone-splitting enzyme (Okayama, H., Honda, M., and Hayaishi, O. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 2254-2257), was purified approximately 4,000-fold from rat liver and characterized. The purified enzyme exhibited a single protein band at the position of Mr = 83,000 upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme split the bond between ADP-ribose and histone H2B or H1, and also acted on ADP-ribosyl pentapeptide (Pro-(ADP-ribosyl)Glu-Pro-Ala-Lys) of H2B but not its deadenylylated derivative, phosphoribosyl pentapeptide. The enzyme cleaved the bond between histone and mono(ADP-ribose), but hardly cleaved the bond with oligo- or poly(ADP-ribose). The enzymatic product was close to, but not identical with, ADP-ribose. The terminal ribose residue, obtained by hydrolysis of the split product by snake venom phosphodiesterase and alkaline phosphatase, was identified as 3-deoxy-D-glycero-pentos-2-ulose by the following gas chromatography-mass spectrometric analyses: 1) the reduced sugar was a mixture of 3-deoxy-threo- and 3-deoxy-erythro-pentitol, and 2) the deuterated reduced sugar was identical with that derived from synthetic 3-deoxy-D-glycero-pentos-2-ulose. This result indicated that the direct product was 5'-ADP-3"-deoxypent-2"-enofuranose, a dehydrated form of ADP-ribose, and that the enzyme is a lyase and not a hydrolase.
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PMID:ADP-ribosyl protein lyase. Purification, properties, and identification of the product. 669 7

Although 5-fluorouracil (FUra) is readily incorporated into RNA, the possibility of its being incorporated into DNA in substantial amounts has only recently been recognized. Examination of nucleic acids prepared from tumor-bearing BALB/c X DBA/8 F1 mice labeled with [3H]FUra in vivo revealed very little alkali-stable, acid-precipitable radioactivity in tumor and only small amounts in intestine. However, substantial amounts were detected in bone marrow. Pretreatment of mice with low-dose thymidine (500 mg/kg) increased the incorporation of FUra into RNA but did not change the amount incorporated into alkali-stable material. The net result was a reduction in the fraction of the total in an alkali-stable form. Formation of DNA containing FUra residues is substantially reduced if the mice receive very high doses of thymidine along with the labeled FUra, presumably through competition from an expanded deoxythymidine triphosphate pool. Bone marrow nucleic acids labeled with 32P and [3H]FUra were analyzed by cesium sulfate gradients. Two distinct peaks of tritium radioactivity were observed that band with 32P radioactivity at the densities of RNA and DNA. Pretreatment with alkali destroyed the (32P/3H)RNA peak, but not the DNA peak. Cesium sulfate-purified DNA containing FUra residues was digested with pancreatic DNase and venom phosphodiesterase. The resulting nucleotides were analyzed by high-pressure liquid chromatography. The majority of the radioactivity cochromatographed with 5-fluorodeoxyuridine monophosphate marker. No radioactivity was detected in the regions corresponding to fluorouridine monophosphate or deoxyuridine monophosphate, although radioactivity was detected cochromatographing with deoxythymidine monophosphate. After digestion with alkaline phosphatase, the majority of the radioactivity cochromatographed with fluorodeoxyuridine (and some thymidine). These results confirm previous observations of FUra incorporation into DNA of tissue culture cells.
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PMID:Incorporation of 5-fluorouracil into murine bone marrow DNA in vivo. 671 87

To investigate the role of protein p3 in bacteriophage phi 29 initiation of replication, we have studied the nature of the covalent linkage between protein p3 and phi 29 DNA. The protein-DNA compound was digested with micrococcal nuclease and pronase resulting in a nucleotidyl-peptide that was further digested by alkaline phosphatase and snake venom phosphodiesterase yielding 5'-dAMP. The DNA-protein linkage is sensitive to alkali. Treatment of the nucleotidyl-peptide with 0.1 M NaOH at 37 degrees C for 3 hr after phosphatase digestion released 5'-dAMP. Hydrolysis of the nucleotidyl-peptide with 5.8 M HCl at 110 degrees C for 90 min yielded O-phosphoserine. These results, together with the sensitivity of the DNA-protein linkage to snake venom phosphodiesterase and its resistance to hydroxylamine, indicate that protein p3 is covalently linked to phi 29 DNA through a phosphoester bond between L-serine and 5'-dAMP, namely a O,5'-deoxyadenylyl-L-serine bond.
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PMID:Protein p3 is linked to the DNA of phage phi 29 through a phosphoester bond between serine and 5'-dAMP. 677 79

1. Novel nucleic-acid-like polymers containing glucose, glucose 'nucleic acid', were isolated from cytoplasmic particles of Ehrlich ascites tumor cells. It is assumed that the basic structure of the polymers is similar to those of known nucleic acids except that their sugar constituents are glucose derivatives instead of ribose or deoxyribose. 2. When the glucose 'nucleic acid' was incubated with venom phosphodiesterase, four kinds of glucose 'nucleotides' containing bases of cytosine, adenine, guanine and thymine were obtained. 3. When the polymers were incubated with both venom phosphodiesterase and alkaline phosphatase, inorganic phosphates of glucose 'nucleotides' were removed and each nucleotide was converted to a glucose 'nucleoside'.
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PMID:Isolation and characterization of nucleic-acid-like polymers containing glucose from Ehrlich ascites tumor cells. 682 66

A reverse-phase high-performance liquid chromatographic method has been developed to determine the sites of reaction and the product distribution of modified salmon sperm DNA. The DNA was reacted with methyl methanesulfonate in neutral solution, and then degraded into deoxyribonucleosides by snake venom phosphodiesterase and alkaline phosphatase. Four products were identified and quantitated: 7-methyldeoxyguanosine (37.1%), 7-methylguanine (7.3%), 3-methyldeoxycytidine (28.8%), and 1-methyldeoxyadenosine (26.8%). This method provides a rapid procedure for analysis of chemically or biochemically modified nucleic acids.
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PMID:Reverse-phase high-performance liquid chromatography of chemically modified DNA. 684 37

Extensive methylation was found upon reaction of N-methyl-N-nitrosourea with dATP. The products of this reaction were purified by repeated anion exchange column chromatography and were found to consist of adenine deoxyribonucleotides methylated on the base moiety, terminal phosphate, or both. Products methylated on the adenine ring were identified by co-migration of acid-hydrolyzed samples with authentic standards on reverse phase high pressure liquid chromatography. Products methylated on the sugar phosphate moiety were identified by digestion with snake venom phosphodiesterase, alkaline phosphatase, or both followed by polyethyleneimine cellulose thin layer chromatography. The results demonstrate production of gamma-phosphate-methyldATP, beta-phosphate-methyl-dADP, 1-methyldATP, and gamma-phosphate-methyl-1-methyldATP as well as the relatively unstable products 3-methyldATP and gamma-phosphate-methyl-3-methyl-dATP. The identities and amounts of products formed during this reaction in vitro are consistent with our finding that cellular deoxyribonucleotide pools are a significant target for N-methyl-N-nitrosourea (Topal, M. D., and Baker, M. S. (1982) Proc. Natl. Acad. Sci. U.S.A. 79, 2211-2215).
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PMID:Reaction of dATP with N-methyl-N-nitrosourea in vitro. 688 67

GTP:mRNA guanylyltransferase, an enzyme that catalyzes the transfer of a GMP residue from GTP to the 5' end of RNA to form a cap structure identified as G(5')pppN-, has been isolated from HeLa cell nuclei. The enzyme has been purified approximately 1000-fold and separated by column chromatography (using DEAE-cellulose, phosphocellulose, Cibacron blue-agarose, and GTP-agarose) from a variety of other activities, including RNA triphosphatase and mRNA (guanine-7)methyltransferase. The reaction product was identified by its resistance to Penicillium nuclease and alkaline phosphatase, sensitivity to venom phosphodiesterase, and electrophoretic and chromatographic mobilities relative to authentic standards. Optimal enzyme activity was obtained at pH 7.5 in the presence of Mn2+ or Mg2+, GTP, and an appropriate acceptor polyribonucleotide. The enzyme was inhibited by elevated concentrations of salt and by sulfhydryl-binding reagents but was unaffected by S-adenosylmethionine or S-adenosylhomocysteine. A molecular weight of 48,500 was estimated by sucrose gradient centrifugation of purified enzyme.
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PMID:Purification and characterization of mRNA guanylyltransferase from HeLa cell nuclei. 735 12

Snake venom phosphodiesterase (SVP) catalyzes the alcoholysis of ATP by primary R-CH2OH alcohols with uncharged R residues, yielding AMP-O-CH2R esterification products. The alcohols compete with water for an SVP-bound adenylyl intermediate. In this study, it has been shown that SVP also catalyzes the reactions of glycerol 2-phosphate and sn-glycerol 3-phosphate with ATP to yield AMP-O-glycerophosphoryl esters. The products were identified by HPLC, the dependency of the reactions on glycerol phosphates, ultraviolet spectroscopy, and conversion to AMP by phosphodiesterase, or to AMP-O-glyceryl esters by alkaline phosphatase. The results demonstrated that R-CH2OH alcohols with negatively charged R residues, as well as secondary alcohols, act as adenylyl acceptors in SVP reactions, thus extending the usefulness of SVP as a tool to produce 5'-nucleotide derivatives. The efficiencies (EA) of glycerol phosphates as adenylyl acceptors were very high at low, millimolar concentrations, but decreased abruptly when the acceptor concentration was increased and, for glycerol 2-phosphate, when Pi or NaCl was present. In contrast, glycerol EA was independent of its own concentration, Pi, and NaCl. The responses of glycerol phosphates indicate that they act as adenylyl acceptors via a mechanism different from uncharged R-CH2OH alcohols. The occurrence of an acceptor-binding enzyme site, specific for negatively charged R residues, and its potential relevance to the in vivo role of 5'-nucleotide phosphodiesterases as 5'-nucleotidyl transferases are discussed.
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PMID:High efficiency of glycerol 2-phosphate and sn-glycerol 3-phosphate as nucleotidyl acceptors in snake venom phosphodiesterase esterifications. Formation of primary and secondary AMP-O-glyceryl and AMP-O-glycerophosphoryl esters and evidence for an acceptor-binding enzyme site. 758 86


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