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Volumn 41, Issue 4, 2008, Pages 305-309

Effect of metal ions on the secondary structure and activity of calf intestine phosphatase

Author keywords

Activity; Calf intestine alkaline phosphatase; Cobaltions; Secondary structure

Indexed keywords


EID: 43249107971     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2008.41.4.305     Document Type: Article
Times cited : (8)

References (29)
  • 1
    • 0008695705 scopus 로고
    • Molercular properties and mechanism of alkaline phosphatase
    • Spiro TG (ed) John Wiley and sons New York
    • Coleman, J. E. and Gettins, P. (1983a) Molercular properties and mechanism of alkaline phosphatase: In Metal Ions in Biology. Spiro TG (ed) John Wiley and sons, New York, pp 153-217.
    • (1983) Metal Ions in Biology , pp. 153-217
    • Coleman, J.E.1    Gettins, P.2
  • 2
    • 0020646899 scopus 로고
    • 65ZnII, 115mCdII, 60CoII, and MgII binding to alkaline phosphatase of Escherichia coli. Structural and functional effects
    • Coleman, J. E., Nakamura, I. and Chlebowski, J. F. (1983) 65ZnII, 115mCdII, 60CoII, and MgII binding to alkaline phosphatase of Escherichia coli. Structural and functional effects. J. Biol. Chem. 258, 386-395.
    • (1983) J. Biol. Chem. , vol.258 , pp. 386-395
    • Coleman, J.E.1    Nakamura, I.2    Chlebowski, J.F.3
  • 4
    • 0029782670 scopus 로고    scopus 로고
    • Production of two extracellular alkaline phosphatases by a psychrophilic arthrobacter strain
    • Prada, P. D., Loveland-Curtze, J. and Brenchley, J. E. (1996) Production of two extracellular alkaline phosphatases by a psychrophilic arthrobacter strain. Appl. Envir. Microbiol.62,3732-3738.
    • (1996) Appl. Envir. Microbiol. , vol.62 , pp. 3732-3738
    • Prada, P.D.1    Loveland-Curtze, J.2    Brenchley, J.E.3
  • 5
    • 0035490891 scopus 로고    scopus 로고
    • Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon py-rococcus abyssi
    • Zappa, S., Rolland, J., Flament, L. D., Gueguen, Y., Boudrant, J. and Dietrich, J. (2001) Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon py-rococcus abyssi. Appl. Envir. Microbiol. 67, 4504-4511.
    • (2001) Appl. Envir. Microbiol. , vol.67 , pp. 4504-4511
    • Zappa, S.1    Rolland, J.2    Flament, L.D.3    Gueguen, Y.4    Boudrant, J.5    Dietrich, J.6
  • 6
    • 36949026481 scopus 로고    scopus 로고
    • Anti-oxidative effect of a protein from cajanus indicus L against acetamino-phen-induced hepato-nephro toxicity
    • Ayantika, G., and Parames, C. S. (2007) Anti-oxidative effect of a protein from cajanus indicus L against acetamino-phen-induced hepato-nephro toxicity. J. Biochem. Mol. Biol. 40, 1039-1049.
    • (2007) J. Biochem. Mol. Biol. , vol.40 , pp. 1039-1049
    • Ayantika, G.1    Parames, C.S.2
  • 7
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures: two-metal ion catalysis
    • Kim, E. E., and Wycko, H. W. (1991) Reaction mechanism of alkaline phosphatase based on crystal structures: two-metal ion catalysis. J. Mol. Biol. 218, 449-464.
    • (1991) J. Mol. Biol. , vol.218 , pp. 449-464
    • Kim, E.E.1    Wycko, H.W.2
  • 8
    • 33745698741 scopus 로고    scopus 로고
    • Structural studies of human alkaline phosphatase in complex with strontium: implication for its secondary effect in bones
    • Llinas, P., Masella, M., Stigbrand, T., Ménez, A., Stura, E. A. and Du, M.H.L. (2006) Structural studies of human alkaline phosphatase in complex with strontium: implication for its secondary effect in bones. Protein Sci. 15, 1691-1700.
    • (2006) Protein Sci , vol.15 , pp. 1691-1700
    • Llinas, P.1    Masella, M.2    Stigbrand, T.3    Ménez, A.4    Stura, E.A.5    Du, M.H.L.6
  • 9
    • 20444506123 scopus 로고    scopus 로고
    • Structural studies of human placental alkaline phosphatase in complex with functional ligands
    • Llinas, P., Stura, E. A., Ménez, A., Kiss, Z., Stigbrand, T., Millan, J. L. and Du, M.H.L. (2005) Structural studies of human placental alkaline phosphatase in complex with functional ligands. J. Mol. Biol. 350, 441-451.
    • (2005) J. Mol. Biol. , vol.350 , pp. 441-451
    • Llinas, P.1    Stura, E.A.2    Ménez, A.3    Kiss, Z.4    Stigbrand, T.5    Millan, J.L.6    Du, M.H.L.7
  • 10
    • 0016190791 scopus 로고
    • Intestinal alkaline phosphatase physical properties and quaternary structure
    • Fosset, M., Chappelet-Tordo, D. and Lazdunski, M. (1974) Intestinal alkaline phosphatase physical properties and quaternary structure. Biochemistry 13, 1783-1787.
    • (1974) Biochemistry , vol.13 , pp. 1783-1787
    • Fosset, M.1    Chappelet-Tordo, D.2    Lazdunski, M.3
  • 11
    • 0000457907 scopus 로고
    • Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents
    • Plock, D. J. and Vallee, B. L. (1962) Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents. Biochemistry 1, 1039-1043.
    • (1962) Biochemistry , vol.1 , pp. 1039-1043
    • Plock, D.J.1    Vallee, B.L.2
  • 12
    • 0030985610 scopus 로고    scopus 로고
    • Dependence of divalent metal ions on phosphotransferase activity of osseous plate alkaline phosphatase
    • Ciancaglini, P., Pizauro, J. M., Leone, F. A. (1997) Dependence of divalent metal ions on phosphotransferase activity of osseous plate alkaline phosphatase. J. Inorg. Biochem. 66, 1-55.
    • (1997) J. Inorg. Biochem , vol.66 , pp. 1-55
    • Ciancaglini, P.1    Pizauro, J.M.2    Leone, F.A.3
  • 13
    • 0017661954 scopus 로고
    • Selective cobalt oxidation as a means to differentiate metal-binding sites of cobalt alkaline phosphatase
    • Richard, A., Anderson, R. A. and Vallee B. L. (1977) Selective cobalt oxidation as a means to differentiate metal-binding sites of cobalt alkaline phosphatase. Biochemistry 16, 4388-4393.
    • (1977) Biochemistry , vol.16 , pp. 4388-4393
    • Richard, A.1    Anderson, R.A.2    Vallee, B.L.3
  • 14
    • 33750833403 scopus 로고    scopus 로고
    • Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy.
    • Mostafa, R. T., Seyed, H. M. and Bijan, R.(2006) Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy. J. Biochem. Mol. Biol. 39, 530-536.
    • (2006) J. Biochem. Mol. Biol. , vol.39 , pp. 530-536
    • Mostafa, R.T.1    Seyed, H.M.2    Bijan, R.3
  • 15
    • 33750819917 scopus 로고    scopus 로고
    • Interaction of native and apo-carbonic nnhydrase with hydrophobic adsorbents: a comparative structure-function study
    • Zahra, S., Saman, H., Bijan, R., and Mohsen, N. G. (2006) Interaction of native and apo-carbonic nnhydrase with hydrophobic adsorbents: a comparative structure-function study. J. Biochem. Mol. Biol. 39, 636-641.
    • (2006) J. Biochem. Mol. Biol. , vol.39 , pp. 636-641
    • Zahra, S.1    Saman, H.2    Bijan, R.3    Mohsen, N.G.4
  • 16
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260.
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 17
    • 0030042763 scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • Greenfield, N. J. (1995) Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal. Biochem. 235, 1-10.
    • (1995) Anal. Biochem , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 18
    • 0027447099 scopus 로고
    • A Self-Consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N. and Woody, R. W. (1993) A Self-Consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209, 32-44.
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 19
    • 9144222674 scopus 로고    scopus 로고
    • Secondary structure of organo-phosphorus hydrolase in solution and in Langmuir-Blodgett film studied by circular dichroism spectroscopy
    • Zheng, J. Y. Celeste, A. C., Vipin, K. R., Cheng, T. C., Joseph, J. D., and Roger, M. L.(2004) Secondary structure of organo-phosphorus hydrolase in solution and in Langmuir-Blodgett film studied by circular dichroism spectroscopy. J. Phys. Chem. B. 108, 17238-17242.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 17238-17242
    • Zheng, J.Y.1    Celeste, A.C.2    Vipin, K.R.3    Cheng, T.C.4    Joseph, J.D.5    Roger, M.L.6
  • 20
    • 0014251790 scopus 로고
    • Metalloenzymes: the entatic nature of their active sites
    • Valle, B. L. and Williams, R. J. P. (1968) Metalloenzymes: the entatic nature of their active sites. Pro. Natl. Acad. Sci. U.S.A. 59, 498-505.
    • (1968) Pro. Natl. Acad. Sci. U.S.A. , vol.59 , pp. 498-505
    • Valle, B.L.1    Williams, R.J.P.2
  • 21
    • 0014376264 scopus 로고
    • Alkaline phosphatase of escherichia coli: composition
    • Simpson, R. T., Vallee, B. L. and Tait, G. H. (1968) Alkaline phosphatase of escherichia coli: composition. Biochemistry 7, 4336-4342.
    • (1968) Biochemistry , vol.7 , pp. 4336-4342
    • Simpson, R.T.1    Vallee, B.L.2    Tait, G.H.3
  • 23
    • 0028286158 scopus 로고
    • Effect of divalent cations on the molecular structure of the GroEL oligome
    • Azem, A., Diamant, S. and Goloubinoff, P. (1994) Effect of divalent cations on the molecular structure of the GroEL oligome. Biochemistry 33, 6671-6675.
    • (1994) Biochemistry , vol.33 , pp. 6671-6675
    • Azem, A.1    Diamant, S.2    Goloubinoff, P.3
  • 25
    • 0031048501 scopus 로고    scopus 로고
    • Requirement for an additional divalent metal cation to activate protein tyrosine kinases
    • Sun, G. and Budde, R. J. A. (1997) Requirement for an additional divalent metal cation to activate protein tyrosine kinases. Biochemistry 36, 2139-2146.
    • (1997) Biochemistry , vol.36 , pp. 2139-2146
    • Sun, G.1    Budde, R.J.A.2
  • 26
    • 0028902892 scopus 로고
    • Phosphorescence reveals a continued slow annealing of the protein core following reactivation of es-cherichia coli alkaline phosphatase.
    • Subramaniam, V., Bergenhem, N.C., Gafni, A. and Steel, D. G. (1995) Phosphorescence reveals a continued slow annealing of the protein core following reactivation of es-cherichia coli alkaline phosphatase. Biochemistry 34, 1133-1136.
    • (1995) Biochemistry , vol.34 , pp. 1133-1136
    • Subramaniam, V.1    Bergenhem, N.C.2    Gafni, A.3    Steel, D.G.4
  • 27
    • 0014231123 scopus 로고
    • The kinetics of the reaction of nitrophenyl phosphates with alkaline phos-phatase from Escherichia coli
    • Trentham, D. R. and Gutfreund, H. (1968) The kinetics of the reaction of nitrophenyl phosphates with alkaline phos-phatase from Escherichia coli. Biochem. J. 106, 455-460.
    • (1968) Biochem. J. , vol.106 , pp. 455-460
    • Trentham, D.R.1    Gutfreund, H.2
  • 28
    • 20444390656 scopus 로고    scopus 로고
    • Metal specificity is correlated with two crucial active site residues in escherichia coli alkaline phosphatase
    • Wang, J., Stieglitz, K. A. and Kantrowitz, E. R. (2005) Metal specificity is correlated with two crucial active site residues in escherichia coli alkaline phosphatase. Biochemistry 44, 8378-8386.
    • (2005) Biochemistry , vol.44 , pp. 8378-8386
    • Wang, J.1    Stieglitz, K.A.2    Kantrowitz, E.R.3
  • 29
    • 0029977146 scopus 로고    scopus 로고
    • Reversible unfolding of eschericha coli alkaline phosphatase: activity site can be reconsitituted by a number of pathways
    • Sailendra, N. S. and Nandini, G. (1996) Reversible unfolding of eschericha coli alkaline phosphatase: activity site can be reconsitituted by a number of pathways. Arch. Biochem. Biophys. 330, 174-180.
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 174-180
    • Sailendra, N.S.1    Nandini, G.2


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