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Volumn 373, Issue 2, 2008, Pages 296-306

A universal competitive fluorescence polarization activity assay for S-adenosylmethionine utilizing methyltransferases

Author keywords

Catechol O methyltransferase; Fluorescence polarization; Methyltransferase; S Adenosylhomocysteine; S Adenosylmethionine

Indexed keywords

ANTIBODIES; FLUORESCENCE; PHENOLS;

EID: 37549057973     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.09.025     Document Type: Article
Times cited : (45)

References (68)
  • 1
    • 0016421339 scopus 로고
    • Biological methylation: Selected aspects
    • Cantoni G.L. Biological methylation: Selected aspects. Annu. Rev. Biochem. 44 (1975) 435-451
    • (1975) Annu. Rev. Biochem. , vol.44 , pp. 435-451
    • Cantoni, G.L.1
  • 3
    • 0026495913 scopus 로고
    • Mammalian small molecule methyltransferases: Their structural and functional features
    • Fujioka M. Mammalian small molecule methyltransferases: Their structural and functional features. Intl. J. Biochem. 24 (1992) 1917-1924
    • (1992) Intl. J. Biochem. , vol.24 , pp. 1917-1924
    • Fujioka, M.1
  • 4
    • 0019224226 scopus 로고
    • S-Adenosyl-l-methionine-dependent macromolecule methyltransferases: Potential targets for the design of chemotherapeutic agents
    • Borchardt R.T. S-Adenosyl-l-methionine-dependent macromolecule methyltransferases: Potential targets for the design of chemotherapeutic agents. J. Med. Chem. 23 (1980) 347-357
    • (1980) J. Med. Chem. , vol.23 , pp. 347-357
    • Borchardt, R.T.1
  • 5
    • 9744251005 scopus 로고    scopus 로고
    • Biochemistry and biology of mammalian DNA methyltransferases
    • Hermann A., Gowher H., and Jeltsch A. Biochemistry and biology of mammalian DNA methyltransferases. Cell. Mol. Life Sci. 61 (2004) 2571-2887
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2571-2887
    • Hermann, A.1    Gowher, H.2    Jeltsch, A.3
  • 6
    • 3142674953 scopus 로고    scopus 로고
    • Structure and function of histone methyltransferases
    • Trievel R.C. Structure and function of histone methyltransferases. Crit. Rev. Eukaryotic Gene Expr. 14 (2004) 147-169
    • (2004) Crit. Rev. Eukaryotic Gene Expr. , vol.14 , pp. 147-169
    • Trievel, R.C.1
  • 7
    • 21244458092 scopus 로고    scopus 로고
    • S-Adenosylmethionine and protein methylation
    • Grillo M.A., and Colombatto S. S-Adenosylmethionine and protein methylation. Amino Acids 28 (2005) 357-362
    • (2005) Amino Acids , vol.28 , pp. 357-362
    • Grillo, M.A.1    Colombatto, S.2
  • 8
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C., and Zhang Y. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6 (2005) 838-849
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 9
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • Klose R.J., and Zhang Y. Regulation of histone methylation by demethylimination and demethylation. Nat. Rev. Mol. Cell Biol. 8 (2007) 307-318
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 307-318
    • Klose, R.J.1    Zhang, Y.2
  • 12
    • 0020699979 scopus 로고
    • Hypomethylation distinguishes genes of some human cancers from their normal counterparts
    • Feinberg A.P., and Vogelstein B. Hypomethylation distinguishes genes of some human cancers from their normal counterparts. Nature 301 (1983) 89-92
    • (1983) Nature , vol.301 , pp. 89-92
    • Feinberg, A.P.1    Vogelstein, B.2
  • 14
    • 0018776724 scopus 로고
    • 5-Methylcytosine content of nuclear DNA during chemical hepatocarcinogenesis and in carcinomas which result
    • Lapeyre J.N., and Becker F.F. 5-Methylcytosine content of nuclear DNA during chemical hepatocarcinogenesis and in carcinomas which result. Biochem. Biophys. Res. Commun. 87 (1979) 698-705
    • (1979) Biochem. Biophys. Res. Commun. , vol.87 , pp. 698-705
    • Lapeyre, J.N.1    Becker, F.F.2
  • 17
    • 0842303035 scopus 로고    scopus 로고
    • An enzyme-coupled colorimetric assay for S-adenosylmethionine-dependent methyltransferases
    • Hendricks C.L., Ross J.R., Pichersky E., Noel J.P., and Zhou Z.S. An enzyme-coupled colorimetric assay for S-adenosylmethionine-dependent methyltransferases. Anal. Biochem. 326 (2004) 100-105
    • (2004) Anal. Biochem. , vol.326 , pp. 100-105
    • Hendricks, C.L.1    Ross, J.R.2    Pichersky, E.3    Noel, J.P.4    Zhou, Z.S.5
  • 18
    • 17444417051 scopus 로고    scopus 로고
    • A general fluorescence-based coupled assay for S-adenosylmethionine-dependent methyltransferases
    • Wang C., Leffler S., Thompson D.H., and Hrycyna C.A. A general fluorescence-based coupled assay for S-adenosylmethionine-dependent methyltransferases. Biochem. Biophys. Res. Commun. 331 (2005) 351-356
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 351-356
    • Wang, C.1    Leffler, S.2    Thompson, D.H.3    Hrycyna, C.A.4
  • 20
    • 3042753797 scopus 로고    scopus 로고
    • Microplate screening assay to identify inhibitors of human catechol-O-methyltransferase
    • Kurkela M., Siiskonen A., Finel M., Tammela P., Taskinen J., and Vuorela P. Microplate screening assay to identify inhibitors of human catechol-O-methyltransferase. Anal. Biochem. 331 (2004) 198-200
    • (2004) Anal. Biochem. , vol.331 , pp. 198-200
    • Kurkela, M.1    Siiskonen, A.2    Finel, M.3    Tammela, P.4    Taskinen, J.5    Vuorela, P.6
  • 21
    • 17444389293 scopus 로고    scopus 로고
    • A nonradioactive DNA methyltransferase assay adaptable to high-throughput screening
    • Woo Y.H., Rajagopalan P.T., and Benkovic S.J. A nonradioactive DNA methyltransferase assay adaptable to high-throughput screening. Anal. Biochem. 340 (2005) 336-340
    • (2005) Anal. Biochem. , vol.340 , pp. 336-340
    • Woo, Y.H.1    Rajagopalan, P.T.2    Benkovic, S.J.3
  • 22
    • 0033773937 scopus 로고    scopus 로고
    • Fluorescence polarization and anisotropy in high throughput screening: Perspectives and primer
    • Owicki J.C. Fluorescence polarization and anisotropy in high throughput screening: Perspectives and primer. J. Biomol. Screen. 5 (2000) 297-306
    • (2000) J. Biomol. Screen. , vol.5 , pp. 297-306
    • Owicki, J.C.1
  • 25
    • 2442482366 scopus 로고    scopus 로고
    • Miniaturized, ultra-high throughput screening of tyrosine kinases using homogeneous, competitive fluorescence immunoassays
    • Beasley J.R., McCoy P.M., Walker T.L., and Dunn D.A. Miniaturized, ultra-high throughput screening of tyrosine kinases using homogeneous, competitive fluorescence immunoassays. Assay Drug Dev. Technol. 2 (2004) 141-151
    • (2004) Assay Drug Dev. Technol. , vol.2 , pp. 141-151
    • Beasley, J.R.1    McCoy, P.M.2    Walker, T.L.3    Dunn, D.A.4
  • 26
    • 0032518347 scopus 로고    scopus 로고
    • A fluorescence polarization competition immunoassay for tyrosine kinases
    • Seethala R., and Menzel R. A fluorescence polarization competition immunoassay for tyrosine kinases. Anal. Biochem. 255 (1998) 257-262
    • (1998) Anal. Biochem. , vol.255 , pp. 257-262
    • Seethala, R.1    Menzel, R.2
  • 27
    • 0037403059 scopus 로고    scopus 로고
    • A homogeneous assay of kinase activity that detects phosphopeptide using fluorescence polarization and zinc
    • Scott J.E., and Carpenter J.W. A homogeneous assay of kinase activity that detects phosphopeptide using fluorescence polarization and zinc. Anal. Biochem. 316 (2003) 82-91
    • (2003) Anal. Biochem. , vol.316 , pp. 82-91
    • Scott, J.E.1    Carpenter, J.W.2
  • 28
    • 0035576787 scopus 로고    scopus 로고
    • Development and validation of a competitive AKT serine/threonine kinase fluorescence polarization assay using a product-specific anti-phospho-serine antibody
    • Turek T.C., Small E.C., Bryant R.W., and Hill W.A. Development and validation of a competitive AKT serine/threonine kinase fluorescence polarization assay using a product-specific anti-phospho-serine antibody. Anal. Biochem. 299 (2001) 45-53
    • (2001) Anal. Biochem. , vol.299 , pp. 45-53
    • Turek, T.C.1    Small, E.C.2    Bryant, R.W.3    Hill, W.A.4
  • 29
    • 0037408498 scopus 로고    scopus 로고
    • Fluorescence polarization immunoassays for metal ions
    • Johnson D.K. Fluorescence polarization immunoassays for metal ions. Comb. Chem. High Throughput Screen. 6 (2003) 245-255
    • (2003) Comb. Chem. High Throughput Screen. , vol.6 , pp. 245-255
    • Johnson, D.K.1
  • 30
    • 0036752780 scopus 로고    scopus 로고
    • Stable, sensitive, fluorescence-based method for detecting camp
    • Hesley J., Daijo J., and Ferguson A.T. Stable, sensitive, fluorescence-based method for detecting camp. BioTechniques 33 (2002) 691-694
    • (2002) BioTechniques , vol.33 , pp. 691-694
    • Hesley, J.1    Daijo, J.2    Ferguson, A.T.3
  • 31
    • 0027396905 scopus 로고
    • Fluorescence polarization immunoassay detection of amphetamine, methamphetamine, and illicit amphetamine analogues
    • Cody J.T., and Schwarzhoff R. Fluorescence polarization immunoassay detection of amphetamine, methamphetamine, and illicit amphetamine analogues. J. Anal. Toxicol. 17 (1993) 23-33
    • (1993) J. Anal. Toxicol. , vol.17 , pp. 23-33
    • Cody, J.T.1    Schwarzhoff, R.2
  • 32
    • 0029035643 scopus 로고
    • Rapid, fully automated measurement of plasma homocyst(e)ine with the Abbott IMx analyzer
    • Shipchandler M.T., and Moore E.G. Rapid, fully automated measurement of plasma homocyst(e)ine with the Abbott IMx analyzer. Clin. Chem. 41 (1995) 991-994
    • (1995) Clin. Chem. , vol.41 , pp. 991-994
    • Shipchandler, M.T.1    Moore, E.G.2
  • 33
    • 70449228544 scopus 로고
    • Enzymatic O-methylation of epinephrine and other catechols
    • Axelrod J., and Tomchick R. Enzymatic O-methylation of epinephrine and other catechols. J. Biol. Chem. 233 (1958) 702-705
    • (1958) J. Biol. Chem. , vol.233 , pp. 702-705
    • Axelrod, J.1    Tomchick, R.2
  • 34
    • 0013886618 scopus 로고
    • Methylation reactions in the formation and metabolism of catecholamines and other biogenic amines
    • Axelrod J. Methylation reactions in the formation and metabolism of catecholamines and other biogenic amines. Pharmacol. Rev. 18 (1966) 95-113
    • (1966) Pharmacol. Rev. , vol.18 , pp. 95-113
    • Axelrod, J.1
  • 35
    • 0018853550 scopus 로고
    • Catecholoestrogens (2- and 4-hydroxyoestrogens): Chemistry, biogenesis, metabolism, occurrence, and physiological significance
    • Ball P., and Knuppen R. Catecholoestrogens (2- and 4-hydroxyoestrogens): Chemistry, biogenesis, metabolism, occurrence, and physiological significance. Acta Endocrinol. Suppl. (Copenh.) 232 (1980) 1-127
    • (1980) Acta Endocrinol. Suppl. (Copenh.) , vol.232 , pp. 1-127
    • Ball, P.1    Knuppen, R.2
  • 36
    • 0016829492 scopus 로고
    • Catechol-O-methyl transferase: Pharmacological aspects and physiological role
    • Guldberg H.C., and Marsden C.A. Catechol-O-methyl transferase: Pharmacological aspects and physiological role. Pharmacol. Rev. 27 (1975) 135-206
    • (1975) Pharmacol. Rev. , vol.27 , pp. 135-206
    • Guldberg, H.C.1    Marsden, C.A.2
  • 38
    • 18044364832 scopus 로고    scopus 로고
    • Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: Structure-activity relationship and molecular-modeling studies
    • Chen D., Wang C.Y., Lambert J.D., Ai N., Welsh W.J., and Yang C.S. Inhibition of human liver catechol-O-methyltransferase by tea catechins and their metabolites: Structure-activity relationship and molecular-modeling studies. Biochem. Pharmacol. 69 (2005) 1523-1531
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 1523-1531
    • Chen, D.1    Wang, C.Y.2    Lambert, J.D.3    Ai, N.4    Welsh, W.J.5    Yang, C.S.6
  • 39
    • 5744248613 scopus 로고    scopus 로고
    • Phytochemicals inhibit catechol-O-methyltransferase activity in cytosolic fractions from healthy human mammary tissues: Implications for catechol estrogen-induced DNA damage
    • van Duursen M.B., Sanderson J.T., de Jong P.C., Kraaij M., and van den Berg M. Phytochemicals inhibit catechol-O-methyltransferase activity in cytosolic fractions from healthy human mammary tissues: Implications for catechol estrogen-induced DNA damage. Toxicol. Sci. 81 (2004) 316-324
    • (2004) Toxicol. Sci. , vol.81 , pp. 316-324
    • van Duursen, M.B.1    Sanderson, J.T.2    de Jong, P.C.3    Kraaij, M.4    van den Berg, M.5
  • 40
    • 0020320008 scopus 로고
    • Kinetic studies on the O-methylation of dopamine by human brain membrane-bound catechol O-methyltransferase
    • Rivett A.J., and Roth J.A. Kinetic studies on the O-methylation of dopamine by human brain membrane-bound catechol O-methyltransferase. Biochemistry 21 (1982) 1740-1742
    • (1982) Biochemistry , vol.21 , pp. 1740-1742
    • Rivett, A.J.1    Roth, J.A.2
  • 41
    • 0014952230 scopus 로고
    • Kinetics of purified catechol O-methyltransferase
    • Flohe L., and Schwabe K.P. Kinetics of purified catechol O-methyltransferase. Biochim. Biophys. Acta 220 (1970) 469-476
    • (1970) Biochim. Biophys. Acta , vol.220 , pp. 469-476
    • Flohe, L.1    Schwabe, K.P.2
  • 42
    • 0014822746 scopus 로고
    • Catechol-O-methyltransferase: II. A new class of inhibitors of catechol-O-methyltransferase; 3,5-Dihydroxy-4-methoxybenzoic acid and related compounds
    • Nikodejevic B., Senoh S., Daly J.W., and Creveling C.R. Catechol-O-methyltransferase: II. A new class of inhibitors of catechol-O-methyltransferase; 3,5-Dihydroxy-4-methoxybenzoic acid and related compounds. J. Pharmacol. Exp. Ther. 174 (1970) 83-93
    • (1970) J. Pharmacol. Exp. Ther. , vol.174 , pp. 83-93
    • Nikodejevic, B.1    Senoh, S.2    Daly, J.W.3    Creveling, C.R.4
  • 44
    • 18144381216 scopus 로고    scopus 로고
    • Improved assay for catechol-O-methyltransferase activity utilizing norepinephrine as an enzymatic substrate and reversed-phase high-performance liquid chromatography with fluorescence detection
    • Aoyama N., Tsunoda M., and Imai K. Improved assay for catechol-O-methyltransferase activity utilizing norepinephrine as an enzymatic substrate and reversed-phase high-performance liquid chromatography with fluorescence detection. J. Chromatogr. A 1074 (2005) 47-51
    • (2005) J. Chromatogr. A , vol.1074 , pp. 47-51
    • Aoyama, N.1    Tsunoda, M.2    Imai, K.3
  • 45
    • 22844452716 scopus 로고    scopus 로고
    • Rapid assay for catechol-O-methyltransferase activity by high-performance liquid chromatography-fluorescence detection
    • Hirano Y., Tsunoda M., Funatsu T., and Imai K. Rapid assay for catechol-O-methyltransferase activity by high-performance liquid chromatography-fluorescence detection. J. Chromatogr. B 819 (2005) 41-46
    • (2005) J. Chromatogr. B , vol.819 , pp. 41-46
    • Hirano, Y.1    Tsunoda, M.2    Funatsu, T.3    Imai, K.4
  • 46
    • 0642340464 scopus 로고    scopus 로고
    • High-performance liquid chromatography-fluorescent assay of catechol-O-methyltransferase activity in rat brain
    • Masuda M., Tsunoda M., and Imai K. High-performance liquid chromatography-fluorescent assay of catechol-O-methyltransferase activity in rat brain. Anal. Bioanal. Chem. 376 (2003) 1069-1073
    • (2003) Anal. Bioanal. Chem. , vol.376 , pp. 1069-1073
    • Masuda, M.1    Tsunoda, M.2    Imai, K.3
  • 47
    • 0030952520 scopus 로고    scopus 로고
    • Hydroxyindole-O-methyltransferase activity assay using high-performance liquid chromatography with fluorometric detection: Determination of melatonin enzymatically formed from N-acetyl serotonin and S-adenosyl-l-methionine
    • Itoh M.T., Hattori A., and Sumi Y. Hydroxyindole-O-methyltransferase activity assay using high-performance liquid chromatography with fluorometric detection: Determination of melatonin enzymatically formed from N-acetyl serotonin and S-adenosyl-l-methionine. J. Chromatogr. B 692 (1997) 217-221
    • (1997) J. Chromatogr. B , vol.692 , pp. 217-221
    • Itoh, M.T.1    Hattori, A.2    Sumi, Y.3
  • 48
    • 0027319680 scopus 로고
    • Fluorometric assay of rat brain N-methyltransferase with 4-methylnicotinamide
    • Sano A., Endo N., and Takitani S. Fluorometric assay of rat brain N-methyltransferase with 4-methylnicotinamide. Biol. Pharm. Bull. 16 (1993) 304-306
    • (1993) Biol. Pharm. Bull. , vol.16 , pp. 304-306
    • Sano, A.1    Endo, N.2    Takitani, S.3
  • 49
    • 0025918509 scopus 로고
    • A nonradioactive assay for N 5-methyltetrahydrofolate-homocysteine methyltransferase (methionine synthase) based on o-phthaldialdehyde derivatization of methionine and fluorescence detection
    • Garras A., Djurhuus R., Christensen B., Lillehaug J.R., and Ueland P.M. A nonradioactive assay for N 5-methyltetrahydrofolate-homocysteine methyltransferase (methionine synthase) based on o-phthaldialdehyde derivatization of methionine and fluorescence detection. Anal. Biochem. 199 (1991) 112-118
    • (1991) Anal. Biochem. , vol.199 , pp. 112-118
    • Garras, A.1    Djurhuus, R.2    Christensen, B.3    Lillehaug, J.R.4    Ueland, P.M.5
  • 50
    • 0030059823 scopus 로고    scopus 로고
    • Assessment of catechol-O-methyltransferase activity and its inhibition in erythrocytes of animals and humans
    • Zurcher G., Da Prada M., and Dingemanse J. Assessment of catechol-O-methyltransferase activity and its inhibition in erythrocytes of animals and humans. Biomed. Chromatogr. 10 (1996) 32-36
    • (1996) Biomed. Chromatogr. , vol.10 , pp. 32-36
    • Zurcher, G.1    Da Prada, M.2    Dingemanse, J.3
  • 51
    • 0019166692 scopus 로고
    • Determination of catecholamines and O-methylated metabolites by reversed-phase high-performance liquid chromatography with fluorimetric detection and its application to enzyme kinetics
    • Schusler-van Hees M.T., and Beijersbergen van Henegouwen G.M. Determination of catecholamines and O-methylated metabolites by reversed-phase high-performance liquid chromatography with fluorimetric detection and its application to enzyme kinetics. J. Chromatogr. 196 (1980) 101-108
    • (1980) J. Chromatogr. , vol.196 , pp. 101-108
    • Schusler-van Hees, M.T.1    Beijersbergen van Henegouwen, G.M.2
  • 52
    • 0025152002 scopus 로고
    • Determination of catechol O-methyltransferase activity in relation to melanin metabolism using high-performance liquid chromatography with fluorimetric detection
    • Smit N.P., Pavel S., Kammeyer A., and Westerhof W. Determination of catechol O-methyltransferase activity in relation to melanin metabolism using high-performance liquid chromatography with fluorimetric detection. Anal. Biochem. 190 (1990) 286-291
    • (1990) Anal. Biochem. , vol.190 , pp. 286-291
    • Smit, N.P.1    Pavel, S.2    Kammeyer, A.3    Westerhof, W.4
  • 53
    • 0032727881 scopus 로고    scopus 로고
    • Radiochemical high-performance liquid chromatographic assay for the determination of catechol O-methyltransferase activity towards various substrates
    • Lautala P., Ulmanen I., and Taskinen J. Radiochemical high-performance liquid chromatographic assay for the determination of catechol O-methyltransferase activity towards various substrates. J. Chromatogr. B 736 (1999) 143-151
    • (1999) J. Chromatogr. B , vol.736 , pp. 143-151
    • Lautala, P.1    Ulmanen, I.2    Taskinen, J.3
  • 54
    • 0021987914 scopus 로고
    • Determination of catechol-O-methyltransferase activity in brain tissue by high-performance liquid chromatography with on-line radiochemical detection
    • Nissinen E. Determination of catechol-O-methyltransferase activity in brain tissue by high-performance liquid chromatography with on-line radiochemical detection. Anal. Biochem. 144 (1985) 247-252
    • (1985) Anal. Biochem. , vol.144 , pp. 247-252
    • Nissinen, E.1
  • 55
    • 33645967818 scopus 로고    scopus 로고
    • Determination of thiopurine S-methyltransferase (TPMT) activity by comparing various normalization factors: Reference values for Estonian population using HPLC-UV assay
    • Oselin K., Anier K., Tamm R., Kallassalu K., and Maeorg U. Determination of thiopurine S-methyltransferase (TPMT) activity by comparing various normalization factors: Reference values for Estonian population using HPLC-UV assay. J. Chromatogr. B 834 (2006) 77-83
    • (2006) J. Chromatogr. B , vol.834 , pp. 77-83
    • Oselin, K.1    Anier, K.2    Tamm, R.3    Kallassalu, K.4    Maeorg, U.5
  • 57
    • 0037172935 scopus 로고    scopus 로고
    • Thiopurine methyltransferase activity: New conditions for reversed-phase high-performance liquid chromatographic assay without extraction and genotypic-phenotypic correlation
    • Anglicheau D., Sanquer S., Loriot M.A., Beaune P., and Thervet E. Thiopurine methyltransferase activity: New conditions for reversed-phase high-performance liquid chromatographic assay without extraction and genotypic-phenotypic correlation. J. Chromatogr. B 773 (2002) 119-127
    • (2002) J. Chromatogr. B , vol.773 , pp. 119-127
    • Anglicheau, D.1    Sanquer, S.2    Loriot, M.A.3    Beaune, P.4    Thervet, E.5
  • 58
    • 0027459284 scopus 로고
    • Assay of phenylethanolamine N-methyltransferase activity using high-performance liquid chromatography with ultraviolet absorbance detection
    • Beaudouin C., Haurat G., Fraisse L., Souppe J., and Renaud B. Assay of phenylethanolamine N-methyltransferase activity using high-performance liquid chromatography with ultraviolet absorbance detection. J. Chromatogr. 613 (1993) 51-58
    • (1993) J. Chromatogr. , vol.613 , pp. 51-58
    • Beaudouin, C.1    Haurat, G.2    Fraisse, L.3    Souppe, J.4    Renaud, B.5
  • 59
    • 0018265992 scopus 로고
    • Determination of O-methylated metabolites of cathecholamines using high-performance liquid chromatography and electrochemical detection
    • Borchardt R.T., Hegazi M.F., and Schowen R.L. Determination of O-methylated metabolites of cathecholamines using high-performance liquid chromatography and electrochemical detection. J. Chromatogr. 152 (1978) 253-259
    • (1978) J. Chromatogr. , vol.152 , pp. 253-259
    • Borchardt, R.T.1    Hegazi, M.F.2    Schowen, R.L.3
  • 60
    • 0028815731 scopus 로고
    • Improved assay of reaction products to quantitate catechol-O-methyltransferase activity by high-performance liquid chromatography with electrochemical detection
    • Reenila I., Tuomainen P., and Mannisto P.T. Improved assay of reaction products to quantitate catechol-O-methyltransferase activity by high-performance liquid chromatography with electrochemical detection. J. Chromatogr. B 663 (1995) 137-142
    • (1995) J. Chromatogr. B , vol.663 , pp. 137-142
    • Reenila, I.1    Tuomainen, P.2    Mannisto, P.T.3
  • 61
    • 0026643211 scopus 로고
    • Application of an organic solvent extraction to the determination of catechol-O-methyltransferase activity by high-performance liquid chromatography in human mononuclear cells
    • Allen E., Myers C., Frank D., Pettigrew A., Thompson S., and Blumer J.L. Application of an organic solvent extraction to the determination of catechol-O-methyltransferase activity by high-performance liquid chromatography in human mononuclear cells. J. Chromatogr. 578 (1992) 175-188
    • (1992) J. Chromatogr. , vol.578 , pp. 175-188
    • Allen, E.1    Myers, C.2    Frank, D.3    Pettigrew, A.4    Thompson, S.5    Blumer, J.L.6
  • 62
    • 0345869923 scopus 로고    scopus 로고
    • A colorimetric assay for catechol-O-methyltransferase
    • Bailey K., Cowling R., Tan E.W., and Webb D. A colorimetric assay for catechol-O-methyltransferase. Bioorg. Med. Chem. 12 (2004) 595-601
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 595-601
    • Bailey, K.1    Cowling, R.2    Tan, E.W.3    Webb, D.4
  • 64
    • 0015521758 scopus 로고
    • Kinetic properties of a soluble catechol O-methyltransferase of human liver
    • Ball P., Knuppen R., Haupt M., and Breuer H. Kinetic properties of a soluble catechol O-methyltransferase of human liver. Eur. J. Biochem. 26 (1972) 560-569
    • (1972) Eur. J. Biochem. , vol.26 , pp. 560-569
    • Ball, P.1    Knuppen, R.2    Haupt, M.3    Breuer, H.4
  • 65
    • 0033827207 scopus 로고    scopus 로고
    • O-Methylation of tea polyphenols catalyzed by human placental cytosolic catechol-O-methyltransferase
    • Zhu B.T., Patel U.K., Cai M.X., and Conney A.H. O-Methylation of tea polyphenols catalyzed by human placental cytosolic catechol-O-methyltransferase. Drug Metab. Dispos. 28 (2000) 1024-1030
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 1024-1030
    • Zhu, B.T.1    Patel, U.K.2    Cai, M.X.3    Conney, A.H.4
  • 66
    • 0028918413 scopus 로고
    • Kinetics of human soluble and membrane-bound catechol O-methyltransferase: A revised mechanism and description of the thermolabile variant of the enzyme
    • Lotta T., Vidgren J., Tilgmann C., Ulmanen I., Melen K., Julkunen I., and Taskinen J. Kinetics of human soluble and membrane-bound catechol O-methyltransferase: A revised mechanism and description of the thermolabile variant of the enzyme. Biochemistry 34 (1995) 4202-4210
    • (1995) Biochemistry , vol.34 , pp. 4202-4210
    • Lotta, T.1    Vidgren, J.2    Tilgmann, C.3    Ulmanen, I.4    Melen, K.5    Julkunen, I.6    Taskinen, J.7
  • 67
    • 37549020911 scopus 로고    scopus 로고
    • A. Capdevila, R.F. Burk, J. Freedman, F. Frantzen, I. Alfheim, C. Wagner, A simple rapid immunoassay for S-adenosylhomocysteine in plasma, J. Nutr. Biochem. (in press).


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