References
- 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
- 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
- Fernely, H. N (1971) Mammalian alkaline phosphatase in enzymes. Boyer PD (ed) Academic Press, New York, pp 417-447
- 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.
- 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 pyrococcus abyssi. Appl. Envir. Microbiol. 67, 4504-4511 https://doi.org/10.1128/AEM.67.10.4504-4511.2001
- Ayantika, G.,and Parames, C. S. (2007) Anti-oxidative effect of a protein from cajanus indicus L against acetaminophen-induced hepato-nephro toxicity. J. Biochem. Mol. Biol. 40, 1039-1049 https://doi.org/10.5483/BMBRep.2007.40.6.1039
- Kim, E. E., and Wycko, H. W. (1991) Reaction mechanism of alkaline phosphatase based on crystal structures: twometal ion catalysis. J. Mol. Biol. 218, 449-464 https://doi.org/10.1016/0022-2836(91)90724-K
- 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 https://doi.org/10.1110/ps.062123806
- Llinas, P., Stura, E. A., Menez, 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 https://doi.org/10.1016/j.jmb.2005.04.068
- Fosset, M., Chappelet-Tordo, D. and Lazdunski, M. (1974) Intestinal alkaline phosphatase physical properties and quaternary structure. Biochemistry 13, 1783-1787 https://doi.org/10.1021/bi00706a001
- 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 https://doi.org/10.1021/bi00912a014
- 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 https://doi.org/10.1016/S0162-0134(96)00145-6
- 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 https://doi.org/10.1021/bi00639a009
- 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 https://doi.org/10.5483/BMBRep.2006.39.5.530
- 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 https://doi.org/10.5483/BMBRep.2006.39.5.636
- 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 https://doi.org/10.1006/abio.2000.4880
- Greenfield, N. J. (1995) Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal. Biochem. 235, 1-10 https://doi.org/10.1006/abio.1996.0084
- 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 https://doi.org/10.1006/abio.1993.1079
- Zheng, J. Y. Celeste, A. C., Vipin, K. R., Cheng, T. C., Joseph, J. D., and Roger, M. L.(2004) Secondary structure of organophosphorus hydrolase in solution and in Langmuir-Blodgett film studied by circular dichroism spectroscopy. J. Phys. Chem. B. 108, 17238-17242 https://doi.org/10.1021/jp0477396
- 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. https://doi.org/10.1073/pnas.59.2.498
- Simpson, R. T., Vallee, B. L. and Tait, G. H. (1968) Alkaline phosphatase of escherichia coli: composition. Biochemistry 7, 4336-4342 https://doi.org/10.1021/bi00852a028
- Anderson, R., Bosron, W., Kennedy, F. and Vallee ,B. (1975) Role of magnesium in escherichia coli alkaline phosphatase. Proc. Natl. Acad. Sci. U.S.A. 72, 2989-2993. https://doi.org/10.1073/pnas.72.8.2989
- Azem, A., Diamant, S. and Goloubinoff, P. (1994) Effect of divalent cations on the molecular structure of the GroEL oligome. Biochemistry 33, 6671-6675 https://doi.org/10.1021/bi00187a037
- Jakob, U., Meyer, I., Bugl, H., Andre, S., Bardwel, J. C. A. and Buchner, J. (1995) Structural organization of procaryotic and eucaryotic Hsp90. J. Biol. Chem. 270, 14412-14419 https://doi.org/10.1074/jbc.270.24.14412
- Sun, G. and Budde, R. J. A. (1997) Requirement for an additional divalent metal cation to activate protein tyrosine kinases. Biochemistry 36, 2139-2146 https://doi.org/10.1021/bi962291n
- 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 escherichia coli alkaline phosphatase. Biochemistry 34, 1133-1136 https://doi.org/10.1021/bi00004a005
- Trentham, D. R. and Gutfreund, H. (1968) The kinetics of the reaction of nitrophenyl phosphates with alkaline phosphatase from Escherichia coli. Biochem. J. 106, 455-460 https://doi.org/10.1042/bj1060455
- 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 https://doi.org/10.1021/bi050155p
- 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 https://doi.org/10.1006/abbi.1996.0239
Cited by
- Unfolding and inactivation of proteins by counterions in protein-nanoparticles interaction vol.145, 2016, https://doi.org/10.1016/j.colsurfb.2016.04.053
- Spectroscopic investigations on the interaction between cadmium telluride semiconductor nanoparticle and bovine alkaline phosphatase pp.1532-2289, 2019, https://doi.org/10.1080/00387010.2018.1561472