메뉴 건너뛰기




Volumn 53, Issue 2, 2012, Pages 99-103

Continuous enzyme-coupled assay of phosphate- or pyrophosphate-releasing enzymes

Author keywords

Coupled assay; DNA polymerases; Phosphate; Pyrophosphate

Indexed keywords

DNA POLYMERASE; HYPOXANTHINE; INORGANIC PYROPHOSPHATASE; INOSINE; PHOSPHATE; PURINE NUCLEOSIDE PHOSPHORYLASE; PYROPHOSPHATE; URIC ACID; XANTHINE OXIDASE;

EID: 84865062996     PISSN: 07366205     EISSN: 19409818     Source Type: Journal    
DOI: 10.2144/000113905     Document Type: Article
Times cited : (23)

References (26)
  • 1
    • 17544398524 scopus 로고    scopus 로고
    • Fluoro-genic and chromogenic chemosensors and reagents for anions
    • Martínez-Máñez, R. and F. Sancenón. 2003. Fluoro-genic and chromogenic chemosensors and reagents for anions. Chem. Rev. 103:4419-4476.
    • (2003) Chem. Rev , vol.103 , pp. 4419-4476
    • Martínez-Máñez, R.1    Sancenón, F.2
  • 3
    • 0023917654 scopus 로고
    • A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay
    • Baykov, A.A., O.A. Evtushenko, and S.M. Avaeva. 1988. A malachite green procedure for or thophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay. Anal. Biochem. 171:266-270.
    • (1988) Anal. Biochem , vol.171 , pp. 266-270
    • Baykov, A.A.1    Evtushenko, O.A.2    Avaeva, S.M.3
  • 4
    • 77949847432 scopus 로고    scopus 로고
    • A universal, fully automated high throughput screening assay for pyrophosphate and phosphate release from enzymatic reactions
    • Pegan, S.D., Y. Tian, V. Sershon, and A.D. Mesecar. 2010. A universal, fully automated high throughput screening assay for pyrophosphate and phosphate release from enzymatic reactions. Comb. Chem. High Troughput Screen. 13: 27-38.
    • (2010) Comb. Chem. High Troughput Screen , vol.13 , pp. 27-38
    • Pegan, S.D.1    Tian, Y.2    Sershon, V.3    Mesecar, A.D.4
  • 5
    • 0022413197 scopus 로고
    • Enzymic determination of inorganic phosphates, organic phosphates and phosphate-liberating enzymes by use of nucleoside phosphorylase-xanthine oxidase (dehydrogenase)-coupled reactions
    • de Groot, H., H. de Groot, and T. Noll. 1985. Enzymic determination of inorganic phosphates, organic phosphates and phosphate-liberating enzymes by use of nucleoside phosphorylase-xanthine oxidase (dehydrogenase)-coupled reactions. Biochem. J. 230:255-260.
    • (1985) Biochem. J , vol.230 , pp. 255-260
    • de Groot, H.1    de Groot, H.2    Noll, T.3
  • 6
    • 0014546530 scopus 로고
    • Kinetic analysis of coupled enzyme assays
    • McClure, W. R. 1969. Kinetic analysis of coupled enzyme assays. Biochemistry 8:2782-2786.
    • (1969) Biochemistry , vol.8 , pp. 2782-2786
    • McClure, W.R.1
  • 7
    • 0016165601 scopus 로고
    • The kinetics of coupled enzyme reactions. Applications to the assay of glucokinase, with glucose 6-phosphate dehydrogenase as coupling enzyme
    • Storer, A.C. and A. Cornish-Bowden. 1974. The kinetics of coupled enzyme reactions. Applications to the assay of glucokinase, with glucose 6-phosphate dehydrogenase as coupling enzyme. Biochem. J. 141:205-209.
    • (1974) Biochem. J , vol.141 , pp. 205-209
    • Storer, A.C.1    Cornish-Bowden, A.2
  • 8
    • 0005539127 scopus 로고
    • Phosphoribosyl pyrophosphate and the measurement on inorganic pyrophosphate in plant tissues
    • Dancer, J.E. and T. ap Rees. 1989. Phosphoribosyl pyrophosphate and the measurement on inorganic pyrophosphate in plant tissues. Planta 17 7:261-264.
    • (1989) Planta , vol.17 , Issue.7 , pp. 261-264
    • Dancer, J.E.1    ap Rees, T.2
  • 9
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb, M.R. 1992. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl. Acad. Sci. USA 89:4884-4887.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 10
    • 0037446435 scopus 로고    scopus 로고
    • A colorimetric assay for inorganic pyrophosphate that is also useful for measuring product accumulation in polymerase chain reactions
    • Tagiri-Endo, M. 2003. A colorimetric assay for inorganic pyrophosphate that is also useful for measuring product accumulation in polymerase chain reactions. Anal. Biochem. 315: 170-174.
    • (2003) Anal. Biochem , vol.315 , pp. 170-174
    • Tagiri-Endo, M.1
  • 11
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C.H. and Y. Subbarow. 1925. The colorimetric determination of phosphorus. J. Biol. C hem. 66:375-400.
    • (1925) J. Biol. C Hem , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 12
    • 0000899673 scopus 로고
    • Enzymatic synthesis of deoxyribonucleic acid: IX. The polymerase formed after T2 bacteriophage infection of Escherichia coli: A new enzyme
    • Aposhian, H.V. and A. Kornberg. 1962. Enzymatic synthesis of deoxyribonucleic acid: IX. The polymerase formed after T2 bacteriophage infection of Escherichia coli: a new enzyme. J. Biol. Chem. 237:519-525.
    • (1962) J. Biol. Chem , vol.237 , pp. 519-525
    • Aposhian, H.V.1    Kornberg, A.2
  • 13
    • 70249098009 scopus 로고    scopus 로고
    • Proteolysis of the proofreading subunit controls the assembly of Escherichia coli DNA polymerase III catalytic core
    • Bressanin, D., A. Stefan, F. Dal Piaz, S. Cianchetta, L. Reggiani, and A. Hochkoeppler. 2009. Proteolysis of the proofreading subunit controls the assembly of Escherichia coli DNA polymerase III catalytic core. Biochim. Biophys. Acta 1794:1606-1615.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1606-1615
    • Bressanin, D.1    Stefan, A.2    Dal Piaz, F.3    Cianchetta, S.4    Reggiani, L.5    Hochkoeppler, A.6
  • 14
    • 0003989568 scopus 로고
    • Uric acid: UV-assay with uricase
    • In H.U. Bergmeyer (Ed.), Verlag Chemie, Weinheim
    • Scheibe, P., E. Bernt, and H.U. Bergmeyer. 1974. Uric acid: UV-assay with uricase, p. 1999-2005. In H.U. Bergmeyer (Ed.), Methoden der Enzymatischen Analyse, Verlag Chemie, Weinheim.
    • (1974) Methoden Der Enzymatischen Analyse , pp. 1999-2005
    • Scheibe, P.1    Bernt, E.2    Bergmeyer, H.U.3
  • 15
    • 0013895571 scopus 로고
    • The enzymic estimation of glutamate and glutamine
    • Sowerby, J.M. and J.H. Ottaway. 1966. The enzymic estimation of glutamate and glutamine. Biochem. J. 99:246-252.
    • (1966) Biochem. J , vol.99 , pp. 246-252
    • Sowerby, J.M.1    Ottaway, J.H.2
  • 16
    • 80051473766 scopus 로고    scopus 로고
    • PGOODs: New plasmids for the co-expression of proteins in Escherichia coli
    • Conte, E., G. Landolf, G. Vincelli, A. Stefan, and A. Hochkoeppler. 2011. pGOODs: new plasmids for the co-expression of proteins in Escherichia coli. Biotechnol. Lett. 33:1815-1821.
    • (2011) Biotechnol. Lett , vol.33 , pp. 1815-1821
    • Conte, E.1    Landolf, G.2    Vincelli, G.3    Stefan, A.4    Hochkoeppler, A.5
  • 17
    • 0037161144 scopus 로고    scopus 로고
    • Hydrolysis of the 5′-p-nitrophenyl ester of TMP by the proofreading exonuclease (ε) subunit of Escherichia coli DNA polymerase III
    • Hamdan, S., E.M. Bulloch, P.R. Tompson, J. L. Beck, J.Y. Yang, J.A. Crowther, P.E. Lilley, P.D. Carr, et al. 2002. Hydrolysis of the 5′-p-nitrophenyl ester of TMP by the proofreading exonuclease (ε) subunit of Escherichia coli DNA polymerase III. Biochemistry 41:5266-5275.
    • (2002) Biochemistry , vol.41 , pp. 5266-5275
    • Hamdan, S.1    Bulloch, E.M.2    Tompson, P.R.3    Beck, J.L.4    Yang, J.Y.5    Crowther, J.A.6    Lilley, P.E.7    Carr, P.D.8
  • 18
    • 0034964053 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant purine nucleoside phosphorylase from Escherichia coli
    • Lee, J., S. Filosa, J. Bonvin, S. Guyon, R.A. Aponte, and J.L. Turnbull. 2001. Expression, purification, and characterization of recombinant purine nucleoside phosphorylase from Escherichia coli. Protein Expr. Purif. 22:180-188.
    • (2001) Protein Expr. Purif , vol.22 , pp. 180-188
    • Lee, J.1    Filosa, S.2    Bonvin, J.3    Guyon, S.4    Aponte, R.A.5    Turnbull, J.L.6
  • 20
    • 0025121103 scopus 로고
    • Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli
    • Polesky, A.H., T.A. Steitz, N.D. Grindley, and C.M. Joyce. 1990. Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. J. Biol. Chem. 265:14579-14591.
    • (1990) J. Biol. Chem , vol.265 , pp. 14579-14591
    • Polesky, A.H.1    Steitz, T.A.2    Grindley, N.D.3    Joyce, C.M.4
  • 21
    • 0016783924 scopus 로고
    • The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I
    • McClure, W.R. and T.M. Jovin. 1975. The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. J. Biol. Chem. 250:4073-4080.
    • (1975) J. Biol. Chem , vol.250 , pp. 4073-4080
    • McClure, W.R.1    Jovin, T.M.2
  • 22
    • 0018876985 scopus 로고
    • Assay of succinate dehydrogenase activity by the tetrazolium method: Evaluation of an improved technique in skeletal muscle fractions
    • Green, J.D. and H.T. Narahara. 1980. Assay of succinate dehydrogenase activity by the tetrazolium method: evaluation of an improved technique in skeletal muscle fractions. J. Histochem. Cytochem. 28:408-412.
    • (1980) J. Histochem. Cytochem , vol.28 , pp. 408-412
    • Green, J.D.1    Narahara, H.T.2
  • 23
    • 0020345697 scopus 로고
    • Bufers of constant ionic strength for studying pH-dependent processes
    • Ellis, K.J. and J.F. Morrison. 1982. Bufers of constant ionic strength for studying pH-dependent processes. Methods Enzymol. 87:405-426.
    • (1982) Methods Enzymol , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 24
    • 84865067284 scopus 로고
    • The ultra-violet absorption spectra of uric acid and of the ultra-filtrate of serum
    • Smith, F.C. 1928. The ultra-violet absorption spectra of uric acid and of the ultra-filtrate of serum. Biochem. J. 22:1499-1503.
    • (1928) Biochem. J , vol.22 , pp. 1499-1503
    • Smith, F.C.1
  • 25
    • 0141621115 scopus 로고    scopus 로고
    • Study of the absorption spectra of albumin and uric acid in the UV region
    • Vasilevskii, A.M., G.A. Konoplev, and N.V. Kornilov. 2001. Study of the absorption spectra of albumin and uric acid in the UV region. J. Opt. Thechnol. 68:928-930.
    • (2001) J. Opt. Thechnol , vol.68 , pp. 928-930
    • Vasilevskii, A.M.1    Konoplev, G.A.2    Kornilov, N.V.3
  • 26
    • 0014010556 scopus 로고
    • Constitutive inorganic pyrophosphatase of Escherichia coli. I. Purification and catalytic properties
    • Josse, J. 1966. Constitutive inorganic pyrophosphatase of Escherichia coli. I. Purification and catalytic properties. J. Biol. Chem. 241:1938-1947
    • (1966) J. Biol. Chem , vol.241 , pp. 1938-1947
    • Josse, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.