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Volumn 16, Issue 1, 1999, Pages 11-18

Kinetic properties of human dopamine sulfotransferase (SULT1A3) expressed in prokaryotic and eukaryotic systems: Comparison with the recombinant enzyme purified from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

DOPAMINE SULFOTRANSFERASE; ENZYME PURIFICATION; ESCHERICHIA COLI; MASS SPECTROMETRY; MERCAPTOETHANOL; SACCHAROMYCES CEREVISIAE; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS; SULFATION;

EID: 0033152067     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1030     Document Type: Article
Times cited : (32)

References (40)
  • 1
    • 0030996250 scopus 로고    scopus 로고
    • Enzymology of human cytosolic sulfotransferases
    • Falany, C. N. (1997) Enzymology of human cytosolic sulfotransferases. FASEB J. 11, 206-216.
    • (1997) FASEB J. , vol.11 , pp. 206-216
    • Falany, C.N.1
  • 2
    • 0032549065 scopus 로고    scopus 로고
    • Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases
    • Coughtrie, M. W. H., Sharp, S., Maxwell, K., and Innes, N. P. (1998) Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases. Chem.-Biol. Interact 109, 3-27.
    • (1998) Chem.-Biol. Interact , vol.109 , pp. 3-27
    • Coughtrie, M.W.H.1    Sharp, S.2    Maxwell, K.3    Innes, N.P.4
  • 3
    • 0031136606 scopus 로고    scopus 로고
    • The importance of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation
    • Klaassen C. D., and Boles J. W. (1997) The importance of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation. FASEB J. 11, 404-418.
    • (1997) FASEB J. , vol.11 , pp. 404-418
    • Klaassen, C.D.1    Boles, J.W.2
  • 4
    • 0030934879 scopus 로고    scopus 로고
    • Bioactivation of mutagens via sulfation
    • Glatt, H. R. (1997) Bioactivation of mutagens via sulfation. FASEB J. 11, 314-321.
    • (1997) FASEB J. , vol.11 , pp. 314-321
    • Glatt, H.R.1
  • 6
    • 0031887611 scopus 로고    scopus 로고
    • Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver
    • Wang, J., Falany, J. L., and Falany, C. N. (1998) Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver. Mol. Pharmacol. 53, 274-282.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 274-282
    • Wang, J.1    Falany, J.L.2    Falany, C.N.3
  • 7
    • 0020047452 scopus 로고
    • Mutiple forms of phenolsulphotransferase in human tissues: Selective inhibition by dichloronitrophenol
    • Rein, G., Glover, V., and Sandler M. (1982) Mutiple forms of phenolsulphotransferase in human tissues: Selective inhibition by dichloronitrophenol. Biochem. Pharmacol. 31, 1893-1897.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 1893-1897
    • Rein, G.1    Glover, V.2    Sandler, M.3
  • 8
    • 0020579139 scopus 로고
    • Thermolabile and thermostable human platelet phenol sulfotransferase: Substrate specificity and physical separation
    • Reiter, C., Mwaluko, G., Dunnette, J., Van Loon, J., and Weinshilboum, R. (1983) Thermolabile and thermostable human platelet phenol sulfotransferase: Substrate specificity and physical separation. Naunyn-Schmiedeberg Arch. Pharmacol. 324, 140-147.
    • (1983) Naunyn-Schmiedeberg Arch. Pharmacol. , vol.324 , pp. 140-147
    • Reiter, C.1    Mwaluko, G.2    Dunnette, J.3    Van Loon, J.4    Weinshilboum, R.5
  • 9
    • 0024309210 scopus 로고
    • Human intestinal phenol sulfotransferase: Assay conditions, activity levels and partial purification of the thermolabile form
    • Sundaram, R. S., Szumlanski, C., Otterness, D., van Loon, J. A., and Weinshilboum, R. M. (1989) Human intestinal phenol sulfotransferase: Assay conditions, activity levels and partial purification of the thermolabile form. Drug Metab. Dispos. 17, 255-264.
    • (1989) Drug Metab. Dispos. , vol.17 , pp. 255-264
    • Sundaram, R.S.1    Szumlanski, C.2    Otterness, D.3    Van Loon, J.A.4    Weinshilboum, R.M.5
  • 10
    • 0029957577 scopus 로고    scopus 로고
    • Design, production and characterisation of antibodies discriminating between the phenol- and monoamine-sulphating forms of human phenol sulphotransferase
    • Rubin, G. L., Sharp, S., Jones, A. L., Glatt, H., Mills, J. A., and Coughtrie, M. W. H. (1996) Design, production and characterisation of antibodies discriminating between the phenol- and monoamine-sulphating forms of human phenol sulphotransferase. Xenobiotica 26, 1113-1119.
    • (1996) Xenobiotica , vol.26 , pp. 1113-1119
    • Rubin, G.L.1    Sharp, S.2    Jones, A.L.3    Glatt, H.4    Mills, J.A.5    Coughtrie, M.W.H.6
  • 11
    • 0029090872 scopus 로고
    • Is there a third peripheral catecholaminergic system? Endogenous dopamine as an autocrine/paracrine substance derived from plasma DOPA and inactivated by conjugation
    • Goldstein, D. S., Mezey, E., Yamamoto, T., Aneman, A., Friberg, P., and Eisenhofer, G. (1995) Is there a third peripheral catecholaminergic system? Endogenous dopamine as an autocrine/paracrine substance derived from plasma DOPA and inactivated by conjugation. Hypertens. Res. 18(Suppl 1), S93-S99.
    • (1995) Hypertens. Res. , vol.18 , Issue.SUPPL. 1
    • Goldstein, D.S.1    Mezey, E.2    Yamamoto, T.3    Aneman, A.4    Friberg, P.5    Eisenhofer, G.6
  • 13
    • 0028898346 scopus 로고
    • Human platelet phenolsulfotransferases - cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form
    • Jones, A. L., Hagen, M., Coughtrie, M. W. H., Roberts, R. C., and Glatt, H. (1995) Human platelet phenolsulfotransferases - cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form. Biochem. Biophys. Res. Commun. 208, 855-862.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 855-862
    • Jones, A.L.1    Hagen, M.2    Coughtrie, M.W.H.3    Roberts, R.C.4    Glatt, H.5
  • 14
    • 0023943785 scopus 로고
    • Triiodothyronine: A substrate for the thermostable and thermolabile forms of human phenol sulfotransferase
    • Young, W. F., Gorman, C. A., and Weinshilboum, R. M. (1988) Triiodothyronine: A substrate for the thermostable and thermolabile forms of human phenol sulfotransferase. Endocrinology 122, 1816-1824.
    • (1988) Endocrinology , vol.122 , pp. 1816-1824
    • Young, W.F.1    Gorman, C.A.2    Weinshilboum, R.M.3
  • 17
    • 0027469416 scopus 로고
    • Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase
    • Wilborn, T. W., Comer, K. A., Dooley, T. P., Reardon, I. M., Heinrikson, R. L., and Falany C. N. (1993) Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase. Mol. Pharmacol. 43, 70-77.
    • (1993) Mol. Pharmacol. , vol.43 , pp. 70-77
    • Wilborn, T.W.1    Comer, K.A.2    Dooley, T.P.3    Reardon, I.M.4    Heinrikson, R.L.5    Falany, C.N.6
  • 18
    • 0028112007 scopus 로고
    • Functional-characterization of 2 human sulfotransferase cDNAs that encode monoamine-sulfating and phenol-sulfating forms of phenol sulfotransferase - Substrate kinetics, thermal-stability and inhibitor-sensitivity studies
    • Veronese, M. E., Burgess, W., Zhu, X. Y., and McManus, M. E. (1994) Functional-characterization of 2 human sulfotransferase cDNAs that encode monoamine-sulfating and phenol-sulfating forms of phenol sulfotransferase - Substrate kinetics, thermal-stability and inhibitor-sensitivity studies. Biochem. J. 302, 497-502.
    • (1994) Biochem. J. , vol.302 , pp. 497-502
    • Veronese, M.E.1    Burgess, W.2    Zhu, X.Y.3    McManus, M.E.4
  • 19
    • 0029051063 scopus 로고
    • Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme
    • Forbes, K. J., Hagen, M., Glatt, H., Hume, R., and Coughtrie, M. W. H. (1995) Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. Mol. Cell. Endocrinol. 112, 53-60.
    • (1995) Mol. Cell. Endocrinol. , vol.112 , pp. 53-60
    • Forbes, K.J.1    Hagen, M.2    Glatt, H.3    Hume, R.4    Coughtrie, M.W.H.5
  • 21
    • 0029053067 scopus 로고
    • Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase
    • Falany, C. N., Krasnykh, V., and Falany, J. L. (1995) Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase. J. Steroid Biochem. Mol. Biol. 52, 529-539.
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.52 , pp. 529-539
    • Falany, C.N.1    Krasnykh, V.2    Falany, J.L.3
  • 22
    • 0030459495 scopus 로고    scopus 로고
    • Improved bacterial expression of the human P form phenolsulfotransferase - Applications to drug metabolism
    • Lewis, A. J., Kelly, M. M., Walle, U. K., Eaton, E. A., Falany, C. N., and Walle, T. (1996) Improved bacterial expression of the human P form phenolsulfotransferase - Applications to drug metabolism. Drug Metab. Dispos. 24, 1180-1185.
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 1180-1185
    • Lewis, A.J.1    Kelly, M.M.2    Walle, U.K.3    Eaton, E.A.4    Falany, C.N.5    Walle, T.6
  • 23
    • 0031259783 scopus 로고    scopus 로고
    • High level expression and characterization of recombinant human hippocampus phenol sulfotransferase: A novel phenol-sulfating form of phenol sulfotransferase
    • Hwang, S.-R., Palkovits, M., and Hook, V. Y. H. (1997) High level expression and characterization of recombinant human hippocampus phenol sulfotransferase: A novel phenol-sulfating form of phenol sulfotransferase. Protein Express. Purif. 11, 125-134.
    • (1997) Protein Express. Purif. , vol.11 , pp. 125-134
    • Hwang, S.-R.1    Palkovits, M.2    Hook, V.Y.H.3
  • 24
    • 0029558167 scopus 로고
    • Salmonella strains and mammalian cells genetically engineered for expression of sulfotransferases
    • Glatt, H., Bartsch, I., Czich, A., Seidel, A., and Falany, C. N. (1995) Salmonella strains and mammalian cells genetically engineered for expression of sulfotransferases. Toxicol. Lett. 82(3), 829-834.
    • (1995) Toxicol. Lett. , vol.82 , Issue.3 , pp. 829-834
    • Glatt, H.1    Bartsch, I.2    Czich, A.3    Seidel, A.4    Falany, C.N.5
  • 28
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983) Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 29
    • 0027495519 scopus 로고
    • The human phenolsulfotransferase polymorphism is determined by the level of expression of the enzyme protein
    • Jones, A. L., Roberts, R. C., and Coughtrie, M. W. H. (1993) The human phenolsulfotransferase polymorphism is determined by the level of expression of the enzyme protein. Biochem. J. 296, 287-290.
    • (1993) Biochem. J. , vol.296 , pp. 287-290
    • Jones, A.L.1    Roberts, R.C.2    Coughtrie, M.W.H.3
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • Hinz, H. J., Ed., Springer Verlag, New York
    • Durchschlag, H. (1986) Specific volumes of biological macromolecules and some other molecules of biological interest, in "TherModynamic Data for Biochemistry and Biotechnology" (Hinz, H. J., Ed.), pp. 45, Springer Verlag, New York.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45
    • Durchschlag, H.1
  • 35
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson, M. L., Correia, J. J., Yphantis, D. A., and Halvorson, H. R. (1981) Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36, 575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 36
    • 0001527730 scopus 로고
    • Rat brain phenolsulfotransferase - Partial purification and some properties
    • Foldes, A., and Meek, J. L. (1973) Rat brain phenolsulfotransferase - Partial purification and some properties. Biochim. Biophys. Acta 327, 365-374.
    • (1973) Biochim. Biophys. Acta , vol.327 , pp. 365-374
    • Foldes, A.1    Meek, J.L.2
  • 37
    • 0023812901 scopus 로고
    • Physical characterization of a monoamine-sulfating form of phenol sulfotransferase from human platelets
    • Heroux, J. A., and Roth, J. A. (1988) Physical characterization of a monoamine-sulfating form of phenol sulfotransferase from human platelets. Mol. Pharmacol. 34, 194-199.
    • (1988) Mol. Pharmacol. , vol.34 , pp. 194-199
    • Heroux, J.A.1    Roth, J.A.2
  • 39
    • 0002447013 scopus 로고
    • The pCI-neo mammalian expression vector
    • Brondyk, W. H. (1995) The pCI-neo mammalian expression vector. Promega Notes 51, 10-13.
    • (1995) Promega Notes , vol.51 , pp. 10-13
    • Brondyk, W.H.1
  • 40
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast: A review
    • Romanos, M. A., Scorer, C. A., and Clare, J. J. (1992) Foreign gene expression in yeast: A review. Yeast 8, 423-488.
    • (1992) Yeast , vol.8 , pp. 423-488
    • Romanos, M.A.1    Scorer, C.A.2    Clare, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.