메뉴 건너뛰기




Volumn 348, Issue 2, 2006, Pages 163-184

The analysis of folate and its metabolic precursors in biological samples

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY;

EID: 29244462972     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.09.017     Document Type: Review
Times cited : (107)

References (229)
  • 1
    • 84965244622 scopus 로고
    • Treatment of "pernicious anaemia of pregnancy" and "tropical nemia"
    • L. Wills Treatment of "pernicious anaemia of pregnancy" and "tropical nemia" Br. Med. J. 1 1931 1059 1064
    • (1931) Br. Med. J. , vol.1 , pp. 1059-1064
    • Wills, L.1
  • 5
    • 0036011084 scopus 로고    scopus 로고
    • Synthesis and turnover of folates in plants
    • A.D. Hanson, and J.F. Gregory Synthesis and turnover of folates in plants Curr. Opin. Plant Biol. 5 2002 244 249
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 244-249
    • Hanson, A.D.1    Gregory, J.F.2
  • 6
    • 14844341424 scopus 로고    scopus 로고
    • Folate synthesis and metabolism in plants and prospects for biofortification
    • G.J.C. Basset, E.P. Quinlivan, J.F. Gregory, and A.D. Hanson Folate synthesis and metabolism in plants and prospects for biofortification Crop Sci. 45 2005 449 453
    • (2005) Crop Sci. , vol.45 , pp. 449-453
    • Basset, G.J.C.1    Quinlivan, E.P.2    Gregory, J.F.3    Hanson, A.D.4
  • 8
    • 0001467691 scopus 로고    scopus 로고
    • Folate metabolism
    • R. Carmel D.W. Jacobsen Cambridge University Press Cambridge, UK
    • R. Cook Folate metabolism R. Carmel D.W. Jacobsen Homocysteine in Health and Disease 2001 Cambridge University Press Cambridge, UK 113 134
    • (2001) Homocysteine in Health and Disease , pp. 113-134
    • Cook, R.1
  • 13
    • 0033970043 scopus 로고    scopus 로고
    • Folate and carcinogenesis: An integrated scheme
    • S.W. Choi, and J.B. Mason Folate and carcinogenesis: an integrated scheme J. Nutr. 130 2000 129 132
    • (2000) J. Nutr. , vol.130 , pp. 129-132
    • Choi, S.W.1    Mason, J.B.2
  • 14
    • 0032704132 scopus 로고    scopus 로고
    • Folate and cancer prevention: A new medical application of folate beyond hyperhomocysteinemia and neural tube defects
    • Y.I. Kim Folate and cancer prevention: a new medical application of folate beyond hyperhomocysteinemia and neural tube defects Nutr. Rev. 57 1999 314 321
    • (1999) Nutr. Rev. , vol.57 , pp. 314-321
    • Kim, Y.I.1
  • 15
    • 0032937408 scopus 로고    scopus 로고
    • Folate deficiency beyond megaloblastic anemia: Hyperhomocysteinemia and other manifestations of dysfunctional folate status
    • R. Green, and J.W. Miller Folate deficiency beyond megaloblastic anemia: hyperhomocysteinemia and other manifestations of dysfunctional folate status Semin. Hematol. 36 1999 47 64
    • (1999) Semin. Hematol. , vol.36 , pp. 47-64
    • Green, R.1    Miller, J.W.2
  • 17
    • 0034068273 scopus 로고    scopus 로고
    • Serum folate and the severity of atrophy of the neocortex in Alzheimer disease: Findings from the Nun Study
    • D.A. Snowdon, C.L. Tully, C.D. Smith, K.P. Riley, and W.R. Markesbery Serum folate and the severity of atrophy of the neocortex in Alzheimer disease: findings from the Nun Study Am. J. Clin. Nutr. 71 2000 993 998
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 993-998
    • Snowdon, D.A.1    Tully, C.L.2    Smith, C.D.3    Riley, K.P.4    Markesbery, W.R.5
  • 19
    • 0023896661 scopus 로고
    • Amino acid biosynthesis inhibitors as herbicides
    • G.M. Kishore, and D.M. Shah Amino acid biosynthesis inhibitors as herbicides Annu. Rev. Biochem. 57 1988 627 663
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 627-663
    • Kishore, G.M.1    Shah, D.M.2
  • 22
    • 14044254160 scopus 로고    scopus 로고
    • A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants
    • S.M.J. Klaus, A. Wegkamp, W. Sybesma, J. Hugenholtz, J.F. Gregory, and A.D. Hanson A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants J. Biol. Chem. 280 2005 5274 5280
    • (2005) J. Biol. Chem. , vol.280 , pp. 5274-5280
    • Klaus, S.M.J.1    Wegkamp, A.2    Sybesma, W.3    Hugenholtz, J.4    Gregory, J.F.5    Hanson, A.D.6
  • 23
    • 0032504243 scopus 로고    scopus 로고
    • Biosynthesis of pteridines in Escherichia coli: Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase
    • C. Haussmann, F. Rohdich, E. Schmidt, A. Bacher, and G. Richter Biosynthesis of pteridines in Escherichia coli: structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase J. Biol. Chem. 273 1998 17418 17424
    • (1998) J. Biol. Chem. , vol.273 , pp. 17418-17424
    • Haussmann, C.1    Rohdich, F.2    Schmidt, E.3    Bacher, A.4    Richter, G.5
  • 24
    • 2442645536 scopus 로고    scopus 로고
    • Folate biosynthesis in higher plants: CDNA cloning, heterologous expression, and characterization of multiple dihydroneopterin aldolases
    • A. Goyer, V. Illarionova, S. Roje, M. Fischer, A. Bacher, and A.D. Hanson Folate biosynthesis in higher plants: cDNA cloning, heterologous expression, and characterization of multiple dihydroneopterin aldolases Plant Physiol. 135 2004 103 111
    • (2004) Plant Physiol. , vol.135 , pp. 103-111
    • Goyer, A.1    Illarionova, V.2    Roje, S.3    Fischer, M.4    Bacher, A.5    Hanson, A.D.6
  • 25
    • 0001870161 scopus 로고    scopus 로고
    • Folate synthesis and compartmentation in higher plants
    • N.J. Kruger S.A. Hill R.G. Ratcliffe Kluwer Dordrecht, Netherlands
    • F. Rébeillé, and R. Douce Folate synthesis and compartmentation in higher plants N.J. Kruger S.A. Hill R.G. Ratcliffe Regulation of Primary Metabolic Pathways in Plants 1999 Kluwer Dordrecht, Netherlands 53 99
    • (1999) Regulation of Primary Metabolic Pathways in Plants , pp. 53-99
    • Rébeillé, F.1    Douce, R.2
  • 26
    • 84954893839 scopus 로고
    • The biosynthesis of folic acid and pteridine cofactor(s) and its regulation
    • W. Pfleiderer Walter de Gruyter Berlin
    • K. Iwai, and M. Kobashi The biosynthesis of folic acid and pteridine cofactor(s) and its regulation W. Pfleiderer Chemistry and Biology of Pterines 1975 Walter de Gruyter Berlin 341 357
    • (1975) Chemistry and Biology of Pterines , pp. 341-357
    • Iwai, K.1    Kobashi, M.2
  • 27
    • 0028809784 scopus 로고
    • Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli
    • V.K. Viswanathan, J.M. Green, and B.P. Nichols Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli J. Bacteriol. 177 1995 5918 5923
    • (1995) J. Bacteriol. , vol.177 , pp. 5918-5923
    • Viswanathan, V.K.1    Green, J.M.2    Nichols, B.P.3
  • 29
    • 0026640790 scopus 로고
    • Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme
    • J.M. Green, W.K. Merkel, and B.P. Nichols Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme J. Bacteriol. 174 1992 5317 5323
    • (1992) J. Bacteriol. , vol.174 , pp. 5317-5323
    • Green, J.M.1    Merkel, W.K.2    Nichols, B.P.3
  • 31
    • 0037743470 scopus 로고    scopus 로고
    • The folate precursor p-aminobenzoate is reversibly converted to its glucose ester in the plant cytosol
    • E.P. Quinlivan, S. Roje, G. Basset, Y. Shachar-Hill, J.F. Gregory, and A.D. Hanson The folate precursor p-aminobenzoate is reversibly converted to its glucose ester in the plant cytosol J. Biol. Chem. 278 2003 20731 20737
    • (2003) J. Biol. Chem. , vol.278 , pp. 20731-20737
    • Quinlivan, E.P.1    Roje, S.2    Basset, G.3    Shachar-Hill, Y.4    Gregory, J.F.5    Hanson, A.D.6
  • 33
    • 84909648141 scopus 로고
    • Kinetic studies of Escherichia coli dihydropteroate synthetase
    • W. Pfleiderer Walter de Gruyter Berlin
    • R. Ferone, and S.R. Webb Kinetic studies of Escherichia coli dihydropteroate synthetase W. Pfleiderer Chemistry and Biology of Pterines 1975 Walter de Gruyter Berlin 61 71
    • (1975) Chemistry and Biology of Pterines , pp. 61-71
    • Ferone, R.1    Webb, S.R.2
  • 34
    • 0006643655 scopus 로고
    • The biosynthesis of folic acid: III. Enzymic formation of dihydrofolic acid from dihydropteroic acid and of tetrahydropteroylpolyglutamic acid compounds from tetrahydrofolic acid
    • M.J. Griffin, and G.M. Brown The biosynthesis of folic acid: III. Enzymic formation of dihydrofolic acid from dihydropteroic acid and of tetrahydropteroylpolyglutamic acid compounds from tetrahydrofolic acid J. Biol. Chem. 239 1964 310 316
    • (1964) J. Biol. Chem. , vol.239 , pp. 310-316
    • Griffin, M.J.1    Brown, G.M.2
  • 35
    • 0035910001 scopus 로고    scopus 로고
    • Tetrahydrofolate biosynthesis in plants: Molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana
    • S. Ravanel, H. Cherest, S. Jabrin, D. Grunwald, Y. Surdin-Kerjan, R. Douce, and F. Rébeillé Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana Proc. Natl. Acad. Sci. USA 98 2001 15360 15365
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15360-15365
    • Ravanel, S.1    Cherest, H.2    Jabrin, S.3    Grunwald, D.4    Surdin-Kerjan, Y.5    Douce, R.6    Rébeillé, F.7
  • 36
    • 0000486275 scopus 로고
    • The biosynthesis of folic acid: I. Substrate and co-factor requirement for enzymatic synthesis by cell free extracts of Escherichia coli
    • G.M. Brown, R.A. Weisman, and D.A. Molner The biosynthesis of folic acid: I. Substrate and co-factor requirement for enzymatic synthesis by cell free extracts of Escherichia coli J. Biol. Chem. 236 1961 2534 2543
    • (1961) J. Biol. Chem. , vol.236 , pp. 2534-2543
    • Brown, G.M.1    Weisman, R.A.2    Molner, D.A.3
  • 37
    • 0024808080 scopus 로고
    • Folylpolyglutamate synthesis and role in the regulation of one-carbon metabolism
    • B. Shane Folylpolyglutamate synthesis and role in the regulation of one-carbon metabolism Vit. Horm. 45 1989 263 335
    • (1989) Vit. Horm. , vol.45 , pp. 263-335
    • Shane, B.1
  • 38
    • 0027520023 scopus 로고
    • Regulation of folate metabolism and one-carbon metabolism in mammalian cells
    • C.B. Osborne, K.E. Lowe, and B. Shane Regulation of folate metabolism and one-carbon metabolism in mammalian cells J. Biol. Chem. 268 1993 21657 21664
    • (1993) J. Biol. Chem. , vol.268 , pp. 21657-21664
    • Osborne, C.B.1    Lowe, K.E.2    Shane, B.3
  • 39
    • 0027485543 scopus 로고
    • Regulation of folate and one-carbon metabolism in mammalian cells: II. Effects of folate-γ-glutamate synthetase substrate specificity and level on folate metabolism and folylpoly-γ-glutamate specificity of metabolic cycles of one-carbon metabolism
    • K.E. Lowe, C.B. Osborne, B.-F. Lin, J.-S. Kim, J.-C. Hsu, and B. Shane Regulation of folate and one-carbon metabolism in mammalian cells: II. Effects of folate-γ-glutamate synthetase substrate specificity and level on folate metabolism and folylpoly-γ-glutamate specificity of metabolic cycles of one-carbon metabolism J. Biol. Chem. 268 1993 21665 21673
    • (1993) J. Biol. Chem. , vol.268 , pp. 21665-21673
    • Lowe, K.E.1    Osborne, C.B.2    Lin, B.-F.3    Kim, J.-S.4    Hsu, J.-C.5    Shane, B.6
  • 40
    • 0026496458 scopus 로고
    • The quantitative analysis of endogenous folate catabolites in human urine
    • J.M. McPartlin, G. Cortney, H. McNulty, D.G. Weir, and J.M. Scott The quantitative analysis of endogenous folate catabolites in human urine Anal. Biochem. 206 1992 256 261
    • (1992) Anal. Biochem. , vol.206 , pp. 256-261
    • McPartlin, J.M.1    Cortney, G.2    McNulty, H.3    Weir, D.G.4    Scott, J.M.5
  • 41
    • 0028972358 scopus 로고
    • Para-Acetamidobenzoylglutamate is a suitable indicator of folate catabolism in rats
    • F. Geoghegan, J.M. McPartlin, D.G. Weir, and J.M. Scott para-Acetamidobenzoylglutamate is a suitable indicator of folate catabolism in rats J. Nutr. 125 1995 2563 2570
    • (1995) J. Nutr. , vol.125 , pp. 2563-2570
    • Geoghegan, F.1    McPartlin, J.M.2    Weir, D.G.3    Scott, J.M.4
  • 42
    • 0015219046 scopus 로고
    • Purification and properties of carboxypeptidase G1
    • J.L. McCullough, B.A. Chabner, and J.R. Bertino Purification and properties of carboxypeptidase G1 J. Biol. Chem. 246 1971 7207 7213
    • (1971) J. Biol. Chem. , vol.246 , pp. 7207-7213
    • McCullough, J.L.1    Chabner, B.A.2    Bertino, J.R.3
  • 43
    • 0018340664 scopus 로고
    • Folate conjugase activity in fresh vegetables and its effect on the determination of free folate content
    • J. Leichter, A.F. Landymore, and C.L. Krumdieck Folate conjugase activity in fresh vegetables and its effect on the determination of free folate content Am. J. Clin. Nutr. 32 1979 92 95
    • (1979) Am. J. Clin. Nutr. , vol.32 , pp. 92-95
    • Leichter, J.1    Landymore, A.F.2    Krumdieck, C.L.3
  • 44
    • 29244445641 scopus 로고    scopus 로고
    • Evidence for salvage of the folate catabolites dihydropterin-6-aldehyde and p-aminobenzoylglutamate in plants [on CD-ROM, 2005 Experimental Biology Meeting abstracts]
    • E.P. Quinlivan, G.J. Basset, J.F. Gregory, and A.D. Hanson Evidence for salvage of the folate catabolites dihydropterin-6-aldehyde and p-aminobenzoylglutamate in plants [on CD-ROM, 2005 Experimental Biology Meeting abstracts] FASEB J. 19 2005 abstract 507.5
    • (2005) FASEB J. , vol.19
    • Quinlivan, E.P.1    Basset, G.J.2    Gregory, J.F.3    Hanson, A.D.4
  • 45
    • 0023097820 scopus 로고
    • Mammalian folylpoly-γ-glutamate synthetase: II. Substrate specificity and kinetic properties
    • D.J. Cichowicz, and B. Shane Mammalian folylpoly-γ-glutamate synthetase: II. Substrate specificity and kinetic properties Biochemistry 26 1987 513 521
    • (1987) Biochemistry , vol.26 , pp. 513-521
    • Cichowicz, D.J.1    Shane, B.2
  • 46
    • 0018954661 scopus 로고
    • Pteroylpoly(γ-glutamate) synthesis by corynebacterium species. Studies on the mechanism of folylpoly(γ-glutamate) synthetase
    • B. Shane Pteroylpoly(γ-glutamate) synthesis by corynebacterium species. Studies on the mechanism of folylpoly(γ-glutamate) synthetase J. Biol. Chem. 255 1980 5663 5667
    • (1980) J. Biol. Chem. , vol.255 , pp. 5663-5667
    • Shane, B.1
  • 47
    • 0021112713 scopus 로고
    • Purification and properties of Lactobacillus casei folylpoly-γ- glutamate synthetase
    • A.L. Bogner, and B. Shane Purification and properties of Lactobacillus casei folylpoly-γ-glutamate synthetase J. Biol. Chem. 258 1983 12574 12581
    • (1983) J. Biol. Chem. , vol.258 , pp. 12574-12581
    • Bogner, A.L.1    Shane, B.2
  • 48
    • 0017712768 scopus 로고
    • Time course study of the in vitro synthesis of avian liver pteroylpoly-γ-glutamates
    • R.W. Thompson, and C.L. Krumdieck Time course study of the in vitro synthesis of avian liver pteroylpoly-γ-glutamates Am. J. Clin. Nutr. 30 1977 1576 1582
    • (1977) Am. J. Clin. Nutr. , vol.30 , pp. 1576-1582
    • Thompson, R.W.1    Krumdieck, C.L.2
  • 49
    • 0016171156 scopus 로고
    • Microbial synthesis of folate polyglutamates from labelled precursors
    • J.P. Brown, F. Dobbs, G.E. Davidson, and J.M. Scott Microbial synthesis of folate polyglutamates from labelled precursors J. Gen. Microbiol. 84 1974 163 171
    • (1974) J. Gen. Microbiol. , vol.84 , pp. 163-171
    • Brown, J.P.1    Dobbs, F.2    Davidson, G.E.3    Scott, J.M.4
  • 50
    • 84909648141 scopus 로고
    • Poly-γ-glutamyl chain lengths in some neutral folates and contributions of folic acid synthesized by intestinal microflora to rat nutrition
    • W. Pfleiderer Walter de Gruyter Berlin
    • C.M. Baugh, E. Braverman, and M.G. Nair Poly-γ-glutamyl chain lengths in some neutral folates and contributions of folic acid synthesized by intestinal microflora to rat nutrition W. Pfleiderer Chemistry and Biology of Pterines 1975 Walter de Gruyter Berlin 465 474
    • (1975) Chemistry and Biology of Pterines , pp. 465-474
    • Baugh, C.M.1    Braverman, E.2    Nair, M.G.3
  • 51
    • 0000083882 scopus 로고
    • Pteroylpolyglutamates: Biosynthesis, degradation, and Function
    • R.L. Blakley S.J. Benkovic Wiley New York
    • J.J. McGuire, and J.K. Coward Pteroylpolyglutamates: Biosynthesis, degradation, and Function R.L. Blakley S.J. Benkovic Folates and Pteridines vol. 1 1984 Wiley New York 135 190
    • (1984) Folates and Pteridines , vol.1 , pp. 135-190
    • McGuire, J.J.1    Coward, J.K.2
  • 52
    • 0018907883 scopus 로고
    • Tetrahydropteroylpolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities
    • R.E. Mackenzie, and C.M. Baugh Tetrahydropteroylpolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities Biochim. Biophys. Acta 611 1980 187 195
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 187-195
    • MacKenzie, R.E.1    Baugh, C.M.2
  • 53
    • 0023129467 scopus 로고
    • Mammalian folylpoly-γ-glutamate synthetase: IV. in vitro and in vivo metabolism of folates and analogues and regulation of folate homeostasis
    • J.D. Cook, D.J. Cichowicz, S. George, A. Lawler, and B. Shane Mammalian folylpoly-γ-glutamate synthetase: IV. In vitro and in vivo metabolism of folates and analogues and regulation of folate homeostasis Biochemistry 26 1987 530 539
    • (1987) Biochemistry , vol.26 , pp. 530-539
    • Cook, J.D.1    Cichowicz, D.J.2    George, S.3    Lawler, A.4    Shane, B.5
  • 55
    • 0000235572 scopus 로고    scopus 로고
    • Determination of folate in cereal-grain food products using trienzyme extraction and combined affinity and reversed-phase liquid chromatography
    • C.M. Pfeiffer, L.M. Rogers, and J.F. Gregory Determination of folate in cereal-grain food products using trienzyme extraction and combined affinity and reversed-phase liquid chromatography J. Agric. Food Chem. 45 1997 407 413
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 407-413
    • Pfeiffer, C.M.1    Rogers, L.M.2    Gregory, J.F.3
  • 56
    • 0027158137 scopus 로고
    • Physico-chemical and biological factors influencing methylfolate stability: Use of dithiothreitol for HPLC analysis with electrochemical detection
    • M.D. Lucock, M. Green, R. Hartley, and M.I. Levene Physico-chemical and biological factors influencing methylfolate stability: use of dithiothreitol for HPLC analysis with electrochemical detection Food Chem. 47 1993 79 86
    • (1993) Food Chem. , vol.47 , pp. 79-86
    • Lucock, M.D.1    Green, M.2    Hartley, R.3    Levene, M.I.4
  • 57
    • 0021026165 scopus 로고
    • Evaluation of ascorbic acid in protecting labile folic acid derivatives
    • S.D. Wilson, and D.W. Horne Evaluation of ascorbic acid in protecting labile folic acid derivatives Proc. Natl. Acad. Sci. USA 80 1980 6500 6504
    • (1980) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6500-6504
    • Wilson, S.D.1    Horne, D.W.2
  • 58
    • 0033674845 scopus 로고    scopus 로고
    • Mechanism of the antimicrobial drug trimethoprim revisited
    • E.P. Quinlivan, J. McPartlin, D.G. Weir, and J. Scott Mechanism of the antimicrobial drug trimethoprim revisited FASEB J. 14 2000 2519 2524
    • (2000) FASEB J. , vol.14 , pp. 2519-2524
    • Quinlivan, E.P.1    McPartlin, J.2    Weir, D.G.3    Scott, J.4
  • 60
    • 15644384258 scopus 로고
    • Adequacy of extraction techniques for determination of folate in foods and other biological materials
    • J.F. Gregory, R. Engelhardt, S.D. Bhandari, D.B. Sartain, and S.K. Gustafson Adequacy of extraction techniques for determination of folate in foods and other biological materials J. Food Comp. Anal. 3 1990 134 144
    • (1990) J. Food Comp. Anal. , vol.3 , pp. 134-144
    • Gregory, J.F.1    Engelhardt, R.2    Bhandari, S.D.3    Sartain, D.B.4    Gustafson, S.K.5
  • 61
    • 0020040461 scopus 로고
    • High performance liquid chromatography of folates: Identification of poly-γ-glutamate chain lengths of labeled and unlabeled folates
    • B. Shane High performance liquid chromatography of folates: identification of poly-γ-glutamate chain lengths of labeled and unlabeled folates Am. J. Clin. Nutr. 35 1982 599 608
    • (1982) Am. J. Clin. Nutr. , vol.35 , pp. 599-608
    • Shane, B.1
  • 62
    • 0017712768 scopus 로고
    • Time course study of the in vivo synthesis of avian liver pteroylpoly-γ-glutamates
    • R.W. Thompson, and C.L. Krumdieck Time course study of the in vivo synthesis of avian liver pteroylpoly-γ-glutamates Am. J. Clin. Nutr. 30 1977 1576 1582
    • (1977) Am. J. Clin. Nutr. , vol.30 , pp. 1576-1582
    • Thompson, R.W.1    Krumdieck, C.L.2
  • 63
    • 0018340996 scopus 로고
    • Separation and identification of pteroylpolyglutamates by polyacrylamide gel chromatography
    • T. Brody, B. Shane, and E.L.R. Stokstad Separation and identification of pteroylpolyglutamates by polyacrylamide gel chromatography Anal. Biochem. 92 1979 501 509
    • (1979) Anal. Biochem. , vol.92 , pp. 501-509
    • Brody, T.1    Shane, B.2    Stokstad, E.L.R.3
  • 64
    • 0018967776 scopus 로고
    • Pteroylpoly(γ-glutamate) synthesis by corynebacterium species: In vitro synthesis of folates
    • B. Shane Pteroylpoly(γ-glutamate) synthesis by corynebacterium species: in vitro synthesis of folates J. Biol. Chem. 255 1980 5649 5654
    • (1980) J. Biol. Chem. , vol.255 , pp. 5649-5654
    • Shane, B.1
  • 65
    • 0016681654 scopus 로고
    • The metabolic consequences of vitamin B-12/methionine deficiency in rats
    • G.E. Davidson, D.G. Weir, and J.M. Scott The metabolic consequences of vitamin B-12/methionine deficiency in rats Biochim. Biophys. Acta 392 1975 207 215
    • (1975) Biochim. Biophys. Acta , vol.392 , pp. 207-215
    • Davidson, G.E.1    Weir, D.G.2    Scott, J.M.3
  • 66
    • 0019255956 scopus 로고
    • An inverse relationship of rat liver folate polyglutamate chain length to nutritional folate sufficiency
    • I.A. Cassady, M.M. Budges, M.J. Healy, and P.F. Nixon An inverse relationship of rat liver folate polyglutamate chain length to nutritional folate sufficiency Biochim. Biophys. Acta 633 1980 258 268
    • (1980) Biochim. Biophys. Acta , vol.633 , pp. 258-268
    • Cassady, I.A.1    Budges, M.M.2    Healy, M.J.3    Nixon, P.F.4
  • 67
    • 0025196288 scopus 로고
    • Modulation of pteroylpolyglutamate concentration and length in response to altered folate nutrition in a comprehensive range of rat tissues
    • G.J. Ward, and P.F. Nixon Modulation of pteroylpolyglutamate concentration and length in response to altered folate nutrition in a comprehensive range of rat tissues J. Nutr. 120 1990 476 484
    • (1990) J. Nutr. , vol.120 , pp. 476-484
    • Ward, G.J.1    Nixon, P.F.2
  • 68
    • 0025362231 scopus 로고
    • Evidence for a localized conversion of endogenous tetrahydrofolate cofactors to dihydrofolate as an important element in antifolate action in murine leukemia cells
    • L.H. Matherly, and S.P. Muench Evidence for a localized conversion of endogenous tetrahydrofolate cofactors to dihydrofolate as an important element in antifolate action in murine leukemia cells Biochem. Pharmacol. 39 1990 2005 2014
    • (1990) Biochem. Pharmacol. , vol.39 , pp. 2005-2014
    • Matherly, L.H.1    Muench, S.P.2
  • 69
    • 0141638790 scopus 로고
    • Physiology of red cells
    • Little, Brown Boston
    • J.H. Jandle Physiology of red cells Blood: Textbook of Haematology 1987 Little, Brown Boston 49 109
    • (1987) Blood: Textbook of Haematology , pp. 49-109
    • Jandle, J.H.1
  • 70
    • 0035197215 scopus 로고    scopus 로고
    • Optimization of erythrocyte folate extraction
    • S.D. O'Broin, and B.P. Kelleher Optimization of erythrocyte folate extraction Clin. Chem. 47 2001 2181 2182
    • (2001) Clin. Chem. , vol.47 , pp. 2181-2182
    • O'Broin, S.D.1    Kelleher, B.P.2
  • 71
    • 0026544977 scopus 로고
    • Microbiological assay on microtitre plates of folate in serum and red cells
    • S.D. O'Broin, and B.P. Kelleher Microbiological assay on microtitre plates of folate in serum and red cells J. Clin. Pathol. 45 1992 344 347
    • (1992) J. Clin. Pathol. , vol.45 , pp. 344-347
    • O'Broin, S.D.1    Kelleher, B.P.2
  • 72
    • 0034975629 scopus 로고    scopus 로고
    • Effect of feeding on circulating micronutrient concentrations in the Burmese python Python molurus
    • S.M. Secor, T.R. Nagy, K.E. Johnston, and T. Tamura Effect of feeding on circulating micronutrient concentrations in the Burmese python Python molurus Comp. Biochem. Physiol. A 129 2001 673 679
    • (2001) Comp. Biochem. Physiol. a , vol.129 , pp. 673-679
    • Secor, S.M.1    Nagy, T.R.2    Johnston, K.E.3    Tamura, T.4
  • 73
    • 0031721774 scopus 로고    scopus 로고
    • Erythrocyte folate analysis: A cause for concern?
    • A.J.A. Wright, P.M. Finglas, and S. Southon Erythrocyte folate analysis: a cause for concern? Clin. Chem. 44 1998 1886 1891
    • (1998) Clin. Chem. , vol.44 , pp. 1886-1891
    • Wright, A.J.A.1    Finglas, P.M.2    Southon, S.3
  • 74
    • 0033634904 scopus 로고    scopus 로고
    • Erythrocyte folate analysis: Saponin added during lysis of whole blood can increase apparent folate concentrations, depending on hemolysate pH
    • A.J.A. Wright, P.M. Finglas, and S. Southon Erythrocyte folate analysis: saponin added during lysis of whole blood can increase apparent folate concentrations, depending on hemolysate pH Clin. Chem. 46 2000 1978 1986
    • (2000) Clin. Chem. , vol.46 , pp. 1978-1986
    • Wright, A.J.A.1    Finglas, P.M.2    Southon, S.3
  • 75
    • 0032573077 scopus 로고    scopus 로고
    • A common mutation in the methylenetetrahydrofolate reductase gene is associated with an accumulation of formylated tetrahydrofolates in red blood cells
    • P.J. Bagley, and J. Selhub A common mutation in the methylenetetrahydrofolate reductase gene is associated with an accumulation of formylated tetrahydrofolates in red blood cells Proc. Natl. Acad. Sci. USA 95 1998 13217 13220
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13217-13220
    • Bagley, P.J.1    Selhub, J.2
  • 76
    • 0022404591 scopus 로고
    • The binding of folyl- and antifolylpolyglutamates to hemoglobin
    • R.E. Benesch, S. Kwong, R. Benesch, and C.M. Baugh The binding of folyl- and antifolylpolyglutamates to hemoglobin J. Biol. Chem. 260 1985 14653 14658
    • (1985) J. Biol. Chem. , vol.260 , pp. 14653-14658
    • Benesch, R.E.1    Kwong, S.2    Benesch, R.3    Baugh, C.M.4
  • 78
    • 0032212438 scopus 로고    scopus 로고
    • Measurable human milk folate is increased by treatment with α-amylase and protease in addition to folate conjugase
    • H.-S. Lim, A.D. Mackey, T. Tamura, S.C. Wong, and M.F. Picciano Measurable human milk folate is increased by treatment with α-amylase and protease in addition to folate conjugase Food Chem. 63 1998 401 407
    • (1998) Food Chem. , vol.63 , pp. 401-407
    • Lim, H.-S.1    MacKey, A.D.2    Tamura, T.3    Wong, S.C.4    Picciano, M.F.5
  • 79
    • 0038128455 scopus 로고    scopus 로고
    • Folate content of foods commonly consumed in Korea measured after trienzyme extraction
    • M. Yon, and T.H. Hyun Folate content of foods commonly consumed in Korea measured after trienzyme extraction Nutr. Res. 23 2003 735 746
    • (2003) Nutr. Res. , vol.23 , pp. 735-746
    • Yon, M.1    Hyun, T.H.2
  • 80
    • 0037300416 scopus 로고    scopus 로고
    • Determination of folate contents in some Australian vegetables
    • Y. Iwatani, J. Arcot, and A.K. Shrestha Determination of folate contents in some Australian vegetables J. Food Compos. Anal. 16 2003 37 48
    • (2003) J. Food Compos. Anal. , vol.16 , pp. 37-48
    • Iwatani, Y.1    Arcot, J.2    Shrestha, A.K.3
  • 83
    • 0019489047 scopus 로고
    • High-pressure liquid chromatography separation and determination of rat liver folates
    • K.E. McMartin, V. Virayotha, and T.R. Tephly High-pressure liquid chromatography separation and determination of rat liver folates Arch. Biochem. Biophys. 209 1981 127 136
    • (1981) Arch. Biochem. Biophys. , vol.209 , pp. 127-136
    • McMartin, K.E.1    Virayotha, V.2    Tephly, T.R.3
  • 84
    • 0033829155 scopus 로고    scopus 로고
    • Folate assay of foods by traditional and tri-enzyme treatments using cryoprotected Lactobacillus casei
    • A.K. Shrestha, J. Arcot, and J. Paterson Folate assay of foods by traditional and tri-enzyme treatments using cryoprotected Lactobacillus casei Food Chem. 71 2000 545 552
    • (2000) Food Chem. , vol.71 , pp. 545-552
    • Shrestha, A.K.1    Arcot, J.2    Paterson, J.3
  • 85
    • 0037438791 scopus 로고    scopus 로고
    • A method for the analysis of natural and synthetic folate in foods
    • R.F. Doherty, and G.R. Beecher A method for the analysis of natural and synthetic folate in foods J. Agric. Food Chem. 51 2003 354 361
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 354-361
    • Doherty, R.F.1    Beecher, G.R.2
  • 86
    • 0022559151 scopus 로고
    • Tissue folate polyglutamate chain length determination by electrophoresis as thymidylate synthase-fluorodeoxyuridylate ternary complex
    • D.G. Priest, and M.T. Doig Tissue folate polyglutamate chain length determination by electrophoresis as thymidylate synthase-fluorodeoxyuridylate ternary complex Methods Enzymol. 122 1986 313 319
    • (1986) Methods Enzymol. , vol.122 , pp. 313-319
    • Priest, D.G.1    Doig, M.T.2
  • 87
    • 0002627902 scopus 로고
    • Adequacy of enzymatic deconjugation in quantification of folate in foods
    • R. Engelhardt, and J.F. Gregory Adequacy of enzymatic deconjugation in quantification of folate in foods J. Agric. Food Chem. 38 1990 154 158
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 154-158
    • Engelhardt, R.1    Gregory, J.F.2
  • 89
    • 0016773259 scopus 로고
    • Folic acid conjugase from plasma: I. Partial purification and properties
    • N. Lakshmaiah, and B.V. Ramasastri Folic acid conjugase from plasma: I. Partial purification and properties Int. J. Vit. Nutr. Res. 45 1975 183 193
    • (1975) Int. J. Vit. Nutr. Res. , vol.45 , pp. 183-193
    • Lakshmaiah, N.1    Ramasastri, B.V.2
  • 90
    • 0000973937 scopus 로고
    • Studies on vitamin Bc conjugase from chicken pancreas
    • V. Mims, and M. Laskowski Studies on vitamin Bc conjugase from chicken pancreas J. Biol. Chem. 160 1945 493 503
    • (1945) J. Biol. Chem. , vol.160 , pp. 493-503
    • Mims, V.1    Laskowski, M.2
  • 91
    • 0019482678 scopus 로고
    • Properties of folic acid γ-glutamyl hydrolase (conjugase) in rat bile and plasma
    • D.W. Horne, C.L. Krumdieck, and C. Wagner Properties of folic acid γ-glutamyl hydrolase (conjugase) in rat bile and plasma J. Nutr. 111 1981 442 449
    • (1981) J. Nutr. , vol.111 , pp. 442-449
    • Horne, D.W.1    Krumdieck, C.L.2    Wagner, C.3
  • 92
    • 0001346367 scopus 로고    scopus 로고
    • Organic acids in selected foods inhibit intestinal brush border pteroylpolyglutamate hydrolase in vitro: Potential mechanism affecting the bioavailability of dietary polyglutamyl folate
    • M.-M. Wei, and J.F. Gregory Organic acids in selected foods inhibit intestinal brush border pteroylpolyglutamate hydrolase in vitro: potential mechanism affecting the bioavailability of dietary polyglutamyl folate J. Agric. Food Chem. 46 1998 211 219
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 211-219
    • Wei, M.-M.1    Gregory, J.F.2
  • 93
    • 0025095497 scopus 로고
    • Inhibition by selected food components of human and porcine intestinal pteroylpolyglutamate hydrolase activity
    • S.D. Bhandari, and J.F. Gregory Inhibition by selected food components of human and porcine intestinal pteroylpolyglutamate hydrolase activity Am. J. Clin. Nutr. 51 1990 87 94
    • (1990) Am. J. Clin. Nutr. , vol.51 , pp. 87-94
    • Bhandari, S.D.1    Gregory, J.F.2
  • 94
    • 0017339246 scopus 로고
    • Studies on the enzymatic hydrolysis of polyglutamyl folates by chicken liver folyl poly-γ-glutamyl carboxypeptidase: I. Intracellular localization, purification, and partial characterization of the enzyme
    • K.N. Rao, and J.M. Noronha Studies on the enzymatic hydrolysis of polyglutamyl folates by chicken liver folyl poly-γ-glutamyl carboxypeptidase: I. Intracellular localization, purification, and partial characterization of the enzyme Biochim. Biophys. Acta 481 1977 594 607
    • (1977) Biochim. Biophys. Acta , vol.481 , pp. 594-607
    • Rao, K.N.1    Noronha, J.M.2
  • 95
    • 29244492468 scopus 로고
    • Determination of folic acid and citrovorum factor in animal tissue
    • L.S. Dietrich, W.J. Monson, H. Gwoh, and C.A. Elvehjem Determination of folic acid and citrovorum factor in animal tissue J. Biol. Chem. 194 1952 549 553
    • (1952) J. Biol. Chem. , vol.194 , pp. 549-553
    • Dietrich, L.S.1    Monson, W.J.2    Gwoh, H.3    Elvehjem, C.A.4
  • 96
    • 29244452776 scopus 로고
    • The use of conjugase preparations in the microbiological assay of folic acid
    • A. Sreenivasan, A.E. Harper, and C.A. Elvehjem The use of conjugase preparations in the microbiological assay of folic acid J. Biol. Chem. 177 1949 117 124
    • (1949) J. Biol. Chem. , vol.177 , pp. 117-124
    • Sreenivasan, A.1    Harper, A.E.2    Elvehjem, C.A.3
  • 97
    • 29244447293 scopus 로고
    • Occurrence and properties of a conjugated form of Leuconostic citrovorum factor
    • V.M. Doctor, and J.R. Couch Occurrence and properties of a conjugated form of Leuconostic citrovorum factor J. Biol. Chem. 200 1953 223 231
    • (1953) J. Biol. Chem. , vol.200 , pp. 223-231
    • Doctor, V.M.1    Couch, J.R.2
  • 98
    • 0000355867 scopus 로고
    • The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid
    • H. Tabor, and L. Wyngarden The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid J. Biol. Chem. 234 1959 1830 1846
    • (1959) J. Biol. Chem. , vol.234 , pp. 1830-1846
    • Tabor, H.1    Wyngarden, L.2
  • 99
    • 0034727672 scopus 로고    scopus 로고
    • Hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate at pH 2.5 to 4.5
    • J.E. Baggott Hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate at pH 2.5 to 4.5 Biochemistry 39 2000 14647 14653
    • (2000) Biochemistry , vol.39 , pp. 14647-14653
    • Baggott, J.E.1
  • 100
    • 0035886740 scopus 로고    scopus 로고
    • High-performance liquid chromatographic measurement of 5,10-methylenetetrahydrofolate in liver
    • D.W. Horne High-performance liquid chromatographic measurement of 5,10-methylenetetrahydrofolate in liver Anal. Biochem. 297 2001 154 159
    • (2001) Anal. Biochem. , vol.297 , pp. 154-159
    • Horne, D.W.1
  • 101
    • 0037315156 scopus 로고    scopus 로고
    • Neither methionine nor nitrous oxide inactivation of methionine synthase affects the concentration of 5,10-methylenetetrahydrofolate in rat liver
    • D.W. Horne Neither methionine nor nitrous oxide inactivation of methionine synthase affects the concentration of 5,10-methylenetetrahydrofolate in rat liver J. Nutr. 133 2003 476 478
    • (2003) J. Nutr. , vol.133 , pp. 476-478
    • Horne, D.W.1
  • 102
    • 0018812587 scopus 로고
    • Enzymatic synthesis of (d)-l-5-methyltetrahydropteroylglutamate of high specific radioactivity
    • D.W. Horne, W.T. Biggs, and C. Wagner Enzymatic synthesis of (d)-l-5-methyltetrahydropteroylglutamate of high specific radioactivity Methods Enzymol. 66 1980 545 547
    • (1980) Methods Enzymol. , vol.66 , pp. 545-547
    • Horne, D.W.1    Biggs, W.T.2    Wagner, C.3
  • 103
    • 0018846778 scopus 로고
    • Preparation and use of affinity columns with bovine milk folate-binding protein (FBP) covalently linked to Sepharose 4B
    • J. Selhub, O. Ahmad, and I.H. Rosenberg Preparation and use of affinity columns with bovine milk folate-binding protein (FBP) covalently linked to Sepharose 4B Methods Enzymol. 66 1980 686 690
    • (1980) Methods Enzymol. , vol.66 , pp. 686-690
    • Selhub, J.1    Ahmad, O.2    Rosenberg, I.H.3
  • 104
    • 0037325815 scopus 로고    scopus 로고
    • Affinity extraction combined with stable isotope dilution LC/MS for the determination of 5-methyltetrahydrofolate in human plasma
    • B.C. Nelson, C.M. Pfeiffer, S.A. Margolis, and C.P. Nelson Affinity extraction combined with stable isotope dilution LC/MS for the determination of 5-methyltetrahydrofolate in human plasma Anal. Biochem. 313 2003 117 127
    • (2003) Anal. Biochem. , vol.313 , pp. 117-127
    • Nelson, B.C.1    Pfeiffer, C.M.2    Margolis, S.A.3    Nelson, C.P.4
  • 105
    • 1442274766 scopus 로고    scopus 로고
    • 5-Methyltetrahydrofolic acid and folic acid measured in plasma with liquid chromatography tandem mass spectrometry: Applications to folate absorption and metabolism
    • R.M. Kok, D.E. Smith, J.R. Dainty, J.T. Van Den Akker, P.M. Finglas, Y.M. Smulders, C. Jakobs, and K. De Meer 5-Methyltetrahydrofolic acid and folic acid measured in plasma with liquid chromatography tandem mass spectrometry: applications to folate absorption and metabolism Anal. Biochem. 326 2004 129 138
    • (2004) Anal. Biochem. , vol.326 , pp. 129-138
    • Kok, R.M.1    Smith, D.E.2    Dainty, J.R.3    Van Den Akker, J.T.4    Finglas, P.M.5    Smulders, Y.M.6    Jakobs, C.7    De Meer, K.8
  • 106
    • 0034118352 scopus 로고    scopus 로고
    • Analysis of folate form distribution by affinity followed by reversed-phase chromatography with electrochemical detection
    • P.J. Bagley, and J. Selhub Analysis of folate form distribution by affinity followed by reversed-phase chromatography with electrochemical detection Clin. Chem. 46 2000 404 411
    • (2000) Clin. Chem. , vol.46 , pp. 404-411
    • Bagley, P.J.1    Selhub, J.2
  • 107
    • 0023911823 scopus 로고
    • Chemical synthesis of deuterated folate monoglutamate and in vivo assessment of urinary excretion of deuterated folates in man
    • J.F. Gregory, and J.P. Toth Chemical synthesis of deuterated folate monoglutamate and in vivo assessment of urinary excretion of deuterated folates in man Anal. Biochem. 170 1988 94 104
    • (1988) Anal. Biochem. , vol.170 , pp. 94-104
    • Gregory, J.F.1    Toth, J.P.2
  • 108
    • 9244238727 scopus 로고    scopus 로고
    • Measurement of folates in serum and conventionally prepared whole blood lysates: Application of an automated 96-well plate isotope-dilution tandem mass spectrometry method
    • Z. Fazili, and C.M. Pfeiffer Measurement of folates in serum and conventionally prepared whole blood lysates: application of an automated 96-well plate isotope-dilution tandem mass spectrometry method Clin. Chem. 50 2004 2378 2381
    • (2004) Clin. Chem. , vol.50 , pp. 2378-2381
    • Fazili, Z.1    Pfeiffer, C.M.2
  • 109
    • 0034947479 scopus 로고    scopus 로고
    • Applicability of microbiological assay and affinity chromatography purification followed by high-performance liquid chromatography (HPLC) in studying folate contents in rye
    • M.S. Kariluoto, L.T. Vahteristo, and V.I. Piironen Applicability of microbiological assay and affinity chromatography purification followed by high-performance liquid chromatography (HPLC) in studying folate contents in rye J. Sci. Food Agric. 81 2001 938 942
    • (2001) J. Sci. Food Agric. , vol.81 , pp. 938-942
    • Kariluoto, M.S.1    Vahteristo, L.T.2    Piironen, V.I.3
  • 110
    • 0024433256 scopus 로고
    • Determination of tissue folate composition by affinity chromatography followed by high-pressure ion pair liquid chromatography
    • J. Selhub Determination of tissue folate composition by affinity chromatography followed by high-pressure ion pair liquid chromatography Anal. Biochem. 182 1989 84 93
    • (1989) Anal. Biochem. , vol.182 , pp. 84-93
    • Selhub, J.1
  • 113
    • 29244478152 scopus 로고    scopus 로고
    • Extraction, purification, and detection by liquid chromatrography- electrospray ionization mass spectrometry of tetrahydrofolate metabolites in Arabidopsis thaliana
    • Z. Chang, and D.A. Gage Extraction, purification, and detection by liquid chromatrography-electrospray ionization mass spectrometry of tetrahydrofolate metabolites in Arabidopsis thaliana Nat. Sci. 1 2003 32 36
    • (2003) Nat. Sci. , vol.1 , pp. 32-36
    • Chang, Z.1    Gage, D.A.2
  • 114
    • 0017838149 scopus 로고
    • Effect of methotrexate on folate binding to a folate binding protein in cow's milk
    • J. Holm, S.I. Hansen, and J. Lyngbye Effect of methotrexate on folate binding to a folate binding protein in cow's milk Acta Pharmacol. Toxicol. 42 1978 77 80
    • (1978) Acta Pharmacol. Toxicol. , vol.42 , pp. 77-80
    • Holm, J.1    Hansen, S.I.2    Lyngbye, J.3
  • 115
    • 0031026794 scopus 로고    scopus 로고
    • Interference by antifolate drugs in a folate competitive protein-binding assay
    • A. Hardcastle, S. Clarke, and W. Aherne Interference by antifolate drugs in a folate competitive protein-binding assay Cancer Chemother. Pharmacol. 39 1997 552 553
    • (1997) Cancer Chemother. Pharmacol. , vol.39 , pp. 552-553
    • Hardcastle, A.1    Clarke, S.2    Aherne, W.3
  • 116
    • 0018831178 scopus 로고
    • Folate assay: Comparison of radioassay and microbiological methods
    • B. Shane, T. Tamura, and E.L.R. Stokstad Folate assay: comparison of radioassay and microbiological methods Clin. Chem. Acta 100 1980 13 19
    • (1980) Clin. Chem. Acta , vol.100 , pp. 13-19
    • Shane, B.1    Tamura, T.2    Stokstad, E.L.R.3
  • 117
    • 0037446436 scopus 로고    scopus 로고
    • Comparison of folate quantification in foods by high-performance liquid chromatography-fluorescence detection to that by stable isotope dilution assays using high-performance liquid chromatography-tandem mass spectrometry
    • A. Freisleben, P. Schieberle, and M. Rychlik Comparison of folate quantification in foods by high-performance liquid chromatography-fluorescence detection to that by stable isotope dilution assays using high-performance liquid chromatography-tandem mass spectrometry Anal. Biochem. 315 2003 247 255
    • (2003) Anal. Biochem. , vol.315 , pp. 247-255
    • Freisleben, A.1    Schieberle, P.2    Rychlik, M.3
  • 118
    • 0032612794 scopus 로고    scopus 로고
    • A validated liquid chromatographic method for determining folates in vegetables, milk powder, liver, and flower
    • E.J.M. Konings A validated liquid chromatographic method for determining folates in vegetables, milk powder, liver, and flower J. AOAC Int. 82 1999 119 127
    • (1999) J. AOAC Int. , vol.82 , pp. 119-127
    • Konings, E.J.M.1
  • 119
    • 0024595789 scopus 로고
    • A rapid and specific extraction procedure for folates determination in rat liver and analysis by high-performance liquid chromatography with fluorometric detection
    • J.C. Gounelle, H. Ladjimi, and P. Prognon A rapid and specific extraction procedure for folates determination in rat liver and analysis by high-performance liquid chromatography with fluorometric detection Anal. Biochem. 176 1989 406 411
    • (1989) Anal. Biochem. , vol.176 , pp. 406-411
    • Gounelle, J.C.1    Ladjimi, H.2    Prognon, P.3
  • 120
    • 0023204646 scopus 로고
    • Trace enrichment of biological folates on solid-phase adsorption cartridges and analysis by high-pressure liquid chromatography
    • T. Rebello Trace enrichment of biological folates on solid-phase adsorption cartridges and analysis by high-pressure liquid chromatography Anal. Biochem. 166 1987 55 64
    • (1987) Anal. Biochem. , vol.166 , pp. 55-64
    • Rebello, T.1
  • 121
    • 0043034057 scopus 로고    scopus 로고
    • Specific and sensitive quantification of folate vitamers in foods by stable isotope dilution assays using high-performance liquid chromatography-tandem mass spectrometry
    • A. Freisleben, P. Schieberle, and M. Rychlik Specific and sensitive quantification of folate vitamers in foods by stable isotope dilution assays using high-performance liquid chromatography-tandem mass spectrometry Anal. Bioanal. Chem. 376 2003 149 156
    • (2003) Anal. Bioanal. Chem. , vol.376 , pp. 149-156
    • Freisleben, A.1    Schieberle, P.2    Rychlik, M.3
  • 122
    • 0346728678 scopus 로고    scopus 로고
    • Solid-phase extraction-electrospray ionization mass spectrometry for the quantification of folate in human plasma or serum
    • B.C. Nelson, C.M. Pfeiffer, S.A. Margolis, and C.P. Nelson Solid-phase extraction-electrospray ionization mass spectrometry for the quantification of folate in human plasma or serum Anal. Biochem. 325 2004 41 51
    • (2004) Anal. Biochem. , vol.325 , pp. 41-51
    • Nelson, B.C.1    Pfeiffer, C.M.2    Margolis, S.A.3    Nelson, C.P.4
  • 123
    • 0742287005 scopus 로고    scopus 로고
    • Determination of folate vitamers in human serum by stable-isotope- dilution tandem mass spectrometry and comparison with radioassay and microbiologic assay
    • C.M. Pfeiffer, Z. Fazili, L. McCoy, M. Zhang, and E.W. Gunter Determination of folate vitamers in human serum by stable-isotope-dilution tandem mass spectrometry and comparison with radioassay and microbiologic assay Clin. Chem. 50 2004 423 432
    • (2004) Clin. Chem. , vol.50 , pp. 423-432
    • Pfeiffer, C.M.1    Fazili, Z.2    McCoy, L.3    Zhang, M.4    Gunter, E.W.5
  • 124
    • 0000243698 scopus 로고
    • Folic acid and biotin synthesis by sulfonamide-sensitive and sulfonaminr-resistant strains of Escherichia coli
    • A.K. Miller Folic acid and biotin synthesis by sulfonamide-sensitive and sulfonaminr-resistant strains of Escherichia coli Proc. Soc. Exp. Biol. Med. 57 1944 151 153
    • (1944) Proc. Soc. Exp. Biol. Med. , vol.57 , pp. 151-153
    • Miller, A.K.1
  • 125
    • 0002009389 scopus 로고
    • The relation of p-aminobenzoic acid to the mechanism of action of sulphanilamide
    • D.D. Woods The relation of p-aminobenzoic acid to the mechanism of action of sulphanilamide Br. J. Exp. Pathol. 21 1940 74 90
    • (1940) Br. J. Exp. Pathol. , vol.21 , pp. 74-90
    • Woods, D.D.1
  • 126
    • 0030744634 scopus 로고    scopus 로고
    • Microbiological assay for serum, plasma, and red cell folate using cryopreserved, microtiter plate method
    • A.M. Molloy, and J.M. Scott Microbiological assay for serum, plasma, and red cell folate using cryopreserved, microtiter plate method Methods Enzymol. 281 1997 43 53
    • (1997) Methods Enzymol. , vol.281 , pp. 43-53
    • Molloy, A.M.1    Scott, J.M.2
  • 127
    • 0022501020 scopus 로고
    • Microbiological analysis of 5-formyltetrahydrofolic acid and other folates using an automatic 96-well plate reader
    • E.M. Newman, and J.F. Tsai Microbiological analysis of 5-formyltetrahydrofolic acid and other folates using an automatic 96-well plate reader Anal. Biochem. 154 1986 509 515
    • (1986) Anal. Biochem. , vol.154 , pp. 509-515
    • Newman, E.M.1    Tsai, J.F.2
  • 129
    • 0026594841 scopus 로고
    • Investigation of the conjugase treatment procedure in the microbiological assay of folate
    • D.M. Goli, and J.T. Vanderslice Investigation of the conjugase treatment procedure in the microbiological assay of folate Food Chem. 43 1992 57 64
    • (1992) Food Chem. , vol.43 , pp. 57-64
    • Goli, D.M.1    Vanderslice, J.T.2
  • 131
    • 0010469445 scopus 로고
    • Microbiological assay of folic acid activity in serum and whole blood
    • J.M. Cooperman Microbiological assay of folic acid activity in serum and whole blood Methods Enzymol. B 18 1971 629 642
    • (1971) Methods Enzymol. B , vol.18 , pp. 629-642
    • Cooperman, J.M.1
  • 132
    • 0036951183 scopus 로고    scopus 로고
    • The effect of different cooking methods on folate retention in various foods that are amongst the major contributors to folate intake in the U.K. diet
    • D.J. McKillop, K. Pentieva, D. Daly, J.M. McPartlin, J. Hughes, J.J. Strain, J.M. Scott, and H. McNulty The effect of different cooking methods on folate retention in various foods that are amongst the major contributors to folate intake in the U.K. diet Br. J. Nutr. 88 2004 681 688
    • (2004) Br. J. Nutr. , vol.88 , pp. 681-688
    • McKillop, D.J.1    Pentieva, K.2    Daly, D.3    McPartlin, J.M.4    Hughes, J.5    Strain, J.J.6    Scott, J.M.7    McNulty, H.8
  • 133
    • 0021884665 scopus 로고
    • The threshold growth response of Lactobacillus casei to 5-methyl-tetrahydrofolic acid: Implications for folate assays
    • A.J.A. Wright, and D.R. Phillips The threshold growth response of Lactobacillus casei to 5-methyl-tetrahydrofolic acid: implications for folate assays Br. J. Nutr. 53 1985 569 573
    • (1985) Br. J. Nutr. , vol.53 , pp. 569-573
    • Wright, A.J.A.1    Phillips, D.R.2
  • 134
    • 0020049944 scopus 로고
    • Studies on the response of Lactobacillus casei to different folate monoglutamates
    • D.R. Phillips, and A.J.A. Wright Studies on the response of Lactobacillus casei to different folate monoglutamates Br. J. Nutr. 47 1982 183 189
    • (1982) Br. J. Nutr. , vol.47 , pp. 183-189
    • Phillips, D.R.1    Wright, A.J.A.2
  • 135
    • 0022559145 scopus 로고
    • Bacterial folylpoly(γ-glutamate) synthase-dihydrofolate synthase
    • A.L. Bogner, and B. Shane Bacterial folylpoly(γ-glutamate) synthase-dihydrofolate synthase Methods Enzymol. 122 1986 349 359
    • (1986) Methods Enzymol. , vol.122 , pp. 349-359
    • Bogner, A.L.1    Shane, B.2
  • 136
    • 0018091378 scopus 로고
    • Effects of antineoplastic drugs on Lactobacillus casei and radioisotopic assays for serum folate
    • R. Carmel Effects of antineoplastic drugs on Lactobacillus casei and radioisotopic assays for serum folate Am. J. Clin. Pathol. 69 1978 137 139
    • (1978) Am. J. Clin. Pathol. , vol.69 , pp. 137-139
    • Carmel, R.1
  • 137
    • 0014138853 scopus 로고
    • Effect of antimicrobial agents on the Lactobacillus casei folate assay
    • M.E.J. Beard, and D.M. Allen Effect of antimicrobial agents on the Lactobacillus casei folate assay Am. J. Clin. Pathol. 48 1967 401 404
    • (1967) Am. J. Clin. Pathol. , vol.48 , pp. 401-404
    • Beard, M.E.J.1    Allen, D.M.2
  • 138
    • 0017816013 scopus 로고
    • Measurement of folates in human plasma and erythrocytes by a radiometric microbiological method
    • M.F. Chen, P.A. McIntyre, and J.A. Kertcher Measurement of folates in human plasma and erythrocytes by a radiometric microbiological method J. Nuclear Med. 19 1978 906 912
    • (1978) J. Nuclear Med. , vol.19 , pp. 906-912
    • Chen, M.F.1    McIntyre, P.A.2    Kertcher, J.A.3
  • 139
    • 0000965380 scopus 로고
    • Sensitivity and Specificity of Enzyme-Immunoassays
    • G. Feldmann P. Druet J. Bignot S. Avrameas North Holland Amsterdam
    • B.K. van Weeman, and A.H.W.M. Schuurs Sensitivity and Specificity of Enzyme-Immunoassays G. Feldmann P. Druet J. Bignot S. Avrameas Immunoenzymatic Techniques 1976 North Holland Amsterdam 125 133
    • (1976) Immunoenzymatic Techniques , pp. 125-133
    • Van Weeman, B.K.1    Schuurs, A.H.W.M.2
  • 140
    • 0023157387 scopus 로고
    • Measurement of low serum and red cell folate levels: Comparison of analytical methods
    • C.R. Gilois, and D.R. Dunbar Measurement of low serum and red cell folate levels: comparison of analytical methods Med. Lab. Sci. 44 1987 33 40
    • (1987) Med. Lab. Sci. , vol.44 , pp. 33-40
    • Gilois, C.R.1    Dunbar, D.R.2
  • 141
    • 0001039280 scopus 로고
    • Cooperative interaction of immobilized folate binding protein with enzyme-folate conjugates: An enzyme-linked assay for folate
    • L.G. Bachas, P.F. Lewis, and M.E. Meyerhoff Cooperative interaction of immobilized folate binding protein with enzyme-folate conjugates: an enzyme-linked assay for folate Anal. Chem. 56 1984 1723 1726
    • (1984) Anal. Chem. , vol.56 , pp. 1723-1726
    • Bachas, L.G.1    Lewis, P.F.2    Meyerhoff, M.E.3
  • 144
    • 0019860511 scopus 로고
    • Radioiodination of pteroyltyrosine: A novel analogue for folate radioassay
    • P.R. Farina, and J.A. Grattan Radioiodination of pteroyltyrosine: a novel analogue for folate radioassay Anal. Biochem. 113 1981 124 129
    • (1981) Anal. Biochem. , vol.113 , pp. 124-129
    • Farina, P.R.1    Grattan, J.A.2
  • 145
    • 0023791449 scopus 로고
    • A competitive enzyme-linked ligand sorbent assay (ELLSA) for quantitation of folates
    • S.I. Hansen, and J. Holm A competitive enzyme-linked ligand sorbent assay (ELLSA) for quantitation of folates Anal. Biochem. 172 1988 160 164
    • (1988) Anal. Biochem. , vol.172 , pp. 160-164
    • Hansen, S.I.1    Holm, J.2
  • 146
    • 49649130702 scopus 로고
    • Estimation of serum folate levels by competitive protein binding assay
    • E.L. Archibald, E.K. Mincey, and T. Morrison Estimation of serum folate levels by competitive protein binding assay Clin. Biochem. 5 1972 232 241
    • (1972) Clin. Biochem. , vol.5 , pp. 232-241
    • Archibald, E.L.1    Mincey, E.K.2    Morrison, T.3
  • 147
    • 0016618179 scopus 로고
    • 3H]pteroylglutamate by charcoal coated with various materials
    • 3H] pteroylglutamate by charcoal coated with various materials Clin. Chem. 21 1975 1927 1931
    • (1975) Clin. Chem. , vol.21 , pp. 1927-1931
    • Zettner, A.1    Duly, P.E.2
  • 148
    • 0030139801 scopus 로고    scopus 로고
    • Homogeneous bioluminescence competitive binding assay for folate based on a coupled glucose-6-phosphate dehydrogenase-bacterial luciferase enzyme system
    • W. Huang, A. Feltus, A. Witkowski, and S. Daunert Homogeneous bioluminescence competitive binding assay for folate based on a coupled glucose-6-phosphate dehydrogenase-bacterial luciferase enzyme system Anal. Chem. 68 1996 1646 1650
    • (1996) Anal. Chem. , vol.68 , pp. 1646-1650
    • Huang, W.1    Feltus, A.2    Witkowski, A.3    Daunert, S.4
  • 149
    • 0016642331 scopus 로고
    • Comparison of commercial kits for radioassay: III. Radioassay of serum folate
    • N.P. Kubasik, M.T. Volosin, and H.E. Sine Comparison of commercial kits for radioassay: III. Radioassay of serum folate Clin. Chem. 21 1975 1922 1926
    • (1975) Clin. Chem. , vol.21 , pp. 1922-1926
    • Kubasik, N.P.1    Volosin, M.T.2    Sine, H.E.3
  • 150
    • 85047687509 scopus 로고    scopus 로고
    • Comparison of five automated serum and whole blood folate asssays
    • W.E. Owen, and W.L. Roberts Comparison of five automated serum and whole blood folate asssays Clin. Chem. 120 2003 121 126
    • (2003) Clin. Chem. , vol.120 , pp. 121-126
    • Owen, W.E.1    Roberts, W.L.2
  • 151
    • 0016768981 scopus 로고
    • Evaluation of a radioassay for serum folate and the effects of ascorbate and methotrexate
    • J. Lindemans, J. van Kapel, and J. Abels Evaluation of a radioassay for serum folate and the effects of ascorbate and methotrexate Clin. Chim. Acta 65 1975 15 20
    • (1975) Clin. Chim. Acta , vol.65 , pp. 15-20
    • Lindemans, J.1    Van Kapel, J.2    Abels, J.3
  • 152
    • 0016584219 scopus 로고
    • PH dependence of the binding of folates to milk binder in radioassay of folate
    • J.K. Givas, and S. Gutcho pH dependence of the binding of folates to milk binder in radioassay of folate Clin. Chem. 21 1975 427 428
    • (1975) Clin. Chem. , vol.21 , pp. 427-428
    • Givas, J.K.1    Gutcho, S.2
  • 153
    • 0022530424 scopus 로고
    • Properties of folate binding protein (FBP) isolated from porcine kidney
    • B.A. Kamen, and J.D. Caston Properties of folate binding protein (FBP) isolated from porcine kidney Biochem. Pharmacol. 35 1986 2323 2329
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 2323-2329
    • Kamen, B.A.1    Caston, J.D.2
  • 155
    • 0036977555 scopus 로고    scopus 로고
    • Evaluation of a radioprotein-binding assay (RPBA) for folate analysis in berries and milk
    • L. Strålsjö, K. Arkbåge, C. Witthöft, and M. Jägerstad Evaluation of a radioprotein-binding assay (RPBA) for folate analysis in berries and milk Food Chem. 79 2002 525 534
    • (2002) Food Chem. , vol.79 , pp. 525-534
    • Strålsjö, L.1    Arkbåge, K.2    Witthöft, C.3    Jägerstad, M.4
  • 156
    • 0019527167 scopus 로고
    • The preparation and properties of folate-binding protein from cow milk
    • D.N. Salter, K.J. Scott, H. Slade, and P. Andrews The preparation and properties of folate-binding protein from cow milk Biochem. J. 193 1981 469 476
    • (1981) Biochem. J. , vol.193 , pp. 469-476
    • Salter, D.N.1    Scott, K.J.2    Slade, H.3    Andrews, P.4
  • 157
    • 0023630297 scopus 로고
    • Immobilized purified folate binding protein: Binding characteristics and use for quantifying folate in erythrocytes
    • S.I. Hansen, J. Holm, and E. Nexo Immobilized purified folate binding protein: binding characteristics and use for quantifying folate in erythrocytes Clin. Chem. 33 1987 1360 1363
    • (1987) Clin. Chem. , vol.33 , pp. 1360-1363
    • Hansen, S.I.1    Holm, J.2    Nexo, E.3
  • 158
    • 0034255382 scopus 로고    scopus 로고
    • Determination of blood folate using acid extraction and internally standardized gas chromatography-mass spectrometry detection
    • S.R. Dueker, Y. Lin, A.D. Jones, R. Mercer, E. Fabbro, J.W. Miller, R. Green, and A. Clifford Determination of blood folate using acid extraction and internally standardized gas chromatography-mass spectrometry detection Anal. Biochem. 283 2000 266 275
    • (2000) Anal. Biochem. , vol.283 , pp. 266-275
    • Dueker, S.R.1    Lin, Y.2    Jones, A.D.3    Mercer, R.4    Fabbro, E.5    Miller, J.W.6    Green, R.7    Clifford, A.8
  • 159
    • 0036467694 scopus 로고    scopus 로고
    • A parallel processing solid phase extraction protocol for determination of whole blood folate
    • Y. Lin, S.R. Dueker, A.D. Jones, and A. Clifford A parallel processing solid phase extraction protocol for determination of whole blood folate Anal. Biochem. 301 2002 14 20
    • (2002) Anal. Biochem. , vol.301 , pp. 14-20
    • Lin, Y.1    Dueker, S.R.2    Jones, A.D.3    Clifford, A.4
  • 160
    • 0037439601 scopus 로고    scopus 로고
    • Human whole blood folate analysis using a selective ion monitoring gas chromatography with mass selective detection protocol
    • Y. Lin, S.R. Dueker, A.D. Jones, and A. Clifford Human whole blood folate analysis using a selective ion monitoring gas chromatography with mass selective detection protocol Anal. Biochem. 312 2003 255 257
    • (2003) Anal. Biochem. , vol.312 , pp. 255-257
    • Lin, Y.1    Dueker, S.R.2    Jones, A.D.3    Clifford, A.4
  • 161
    • 0028855722 scopus 로고
    • Quantitation of red blood cell folates by stable isotope dilution gas chromatography-mass spectrometry utilizing a folate internal standard
    • C.R. Santhosh-Kumar, J.C. Deutsch, K.L. Hassell, N.M. Kolhouse, and J.F. Kolhouse Quantitation of red blood cell folates by stable isotope dilution gas chromatography-mass spectrometry utilizing a folate internal standard Anal. Biochem. 225 1995 1 9
    • (1995) Anal. Biochem. , vol.225 , pp. 1-9
    • Santhosh-Kumar, C.R.1    Deutsch, J.C.2    Hassell, K.L.3    Kolhouse, N.M.4    Kolhouse, J.F.5
  • 162
    • 0348226969 scopus 로고    scopus 로고
    • Determination of total folates in plant material by chemical conversion into para-aminobenzoic acid followed by high performance liquid chromatography combined with on-line postcolumn derivatization and fluorescence detection
    • G.-F. Zhang, K.E. Maudens, S. Storozhenko, K.A. Mortimer, D. Van Der Straeten, and W.E. Lambert Determination of total folates in plant material by chemical conversion into para-aminobenzoic acid followed by high performance liquid chromatography combined with on-line postcolumn derivatization and fluorescence detection J. Agric. Food Chem. 51 2003 7872 7878
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 7872-7878
    • Zhang, G.-F.1    Maudens, K.E.2    Storozhenko, S.3    Mortimer, K.A.4    Van Der Straeten, D.5    Lambert, W.E.6
  • 163
    • 34447125173 scopus 로고    scopus 로고
    • Determination of total folate in human red cells by internally standardized HPLC-tandem mass spectrometry detection [on CD-ROM, 2005 Experimental Biology Meeting abstracts]
    • J.E. Owens, D.M. Holstege, and A.J. Clifford Determination of total folate in human red cells by internally standardized HPLC-tandem mass spectrometry detection [on CD-ROM, 2005 Experimental Biology Meeting abstracts] FASEB J. 19 2005 abstract 271.4
    • (2005) FASEB J. , vol.19
    • Owens, J.E.1    Holstege, D.M.2    Clifford, A.J.3
  • 164
    • 0027999526 scopus 로고
    • 5-Formyltetrahydropteroyl-polyglutamates are the major folate derivatives in Neurospora crassa conidiospores
    • H.L. Kruschwitz, D. McDonald, E.A. Cossins, and V. Schirch 5-Formyltetrahydropteroyl-polyglutamates are the major folate derivatives in Neurospora crassa conidiospores J. Biol. Chem. 269 1994 28757 28763
    • (1994) J. Biol. Chem. , vol.269 , pp. 28757-28763
    • Kruschwitz, H.L.1    McDonald, D.2    Cossins, E.A.3    Schirch, V.4
  • 166
    • 0019548370 scopus 로고
    • Determination of folacin derivatives in selected foods by high-performance liquid chromatography
    • B.P. Day, and J.F. Gregory Determination of folacin derivatives in selected foods by high-performance liquid chromatography J. Agric. Food Chem. 29 1981 374 377
    • (1981) J. Agric. Food Chem. , vol.29 , pp. 374-377
    • Day, B.P.1    Gregory, J.F.2
  • 167
    • 0023060679 scopus 로고
    • Microdetermination of folate monoglutamates in serum by liquid chromatography with electrochemical detection
    • M. Kohashi, K. Inoue, H. Sotobayashi, and K. Iwai Microdetermination of folate monoglutamates in serum by liquid chromatography with electrochemical detection J. Chromatogr. 382 1986 303 307
    • (1986) J. Chromatogr. , vol.382 , pp. 303-307
    • Kohashi, M.1    Inoue, K.2    Sotobayashi, H.3    Iwai, K.4
  • 168
    • 0032730177 scopus 로고    scopus 로고
    • Analysis of some folate monoglutamates by high-performance liquid chromatography-mass spectrometry (part I)
    • P. Stokes, and K. Webb Analysis of some folate monoglutamates by high-performance liquid chromatography-mass spectrometry (part I) J. Chromatogr. A 864 1999 59 67
    • (1999) J. Chromatogr. a , vol.864 , pp. 59-67
    • Stokes, P.1    Webb, K.2
  • 169
    • 0034830356 scopus 로고    scopus 로고
    • A quantitative stable-isotope LC-MS method for the determination of folic acid in fortified foods
    • R.J. Pawlosky, and V.P. Flanagan A quantitative stable-isotope LC-MS method for the determination of folic acid in fortified foods J. Agric. Food Chem. 49 2001 1282 1286
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 1282-1286
    • Pawlosky, R.J.1    Flanagan, V.P.2
  • 170
    • 0035892636 scopus 로고    scopus 로고
    • Determination of 5-methyltetrahydrofolic acid in human serum by stable-isotope dilution high-performance liquid chromatography-mass spectrometry
    • R.J. Pawlosky, V.P. Flanagan, and C.M. Pfeiffer Determination of 5-methyltetrahydrofolic acid in human serum by stable-isotope dilution high-performance liquid chromatography-mass spectrometry Anal. Biochem. 298 2001 299 305
    • (2001) Anal. Biochem. , vol.298 , pp. 299-305
    • Pawlosky, R.J.1    Flanagan, V.P.2    Pfeiffer, C.M.3
  • 171
    • 0035951031 scopus 로고    scopus 로고
    • Preliminary application of liquid chromatography-electrospray-ionization mass spectrometry to the detection of 5-methyltetrahydrofolic acid monoglutamate in human plasma
    • B.C. Nelson, J.J. Dalluge, and S.A. Margolis Preliminary application of liquid chromatography-electrospray-ionization mass spectrometry to the detection of 5-methyltetrahydrofolic acid monoglutamate in human plasma J. Chromatogr. B 765 2001 141 150
    • (2001) J. Chromatogr. B , vol.765 , pp. 141-150
    • Nelson, B.C.1    Dalluge, J.J.2    Margolis, S.A.3
  • 172
    • 0035891168 scopus 로고    scopus 로고
    • Determination of folates in human plasma using hydrophilic interaction chromatography-tandem mass spectrometry
    • S.D. Garbis, A. Melse-Boonstra, C.E. West, and R.B. van Breemen Determination of folates in human plasma using hydrophilic interaction chromatography-tandem mass spectrometry Anal. Chem. 73 2001 5358 5364
    • (2001) Anal. Chem. , vol.73 , pp. 5358-5364
    • Garbis, S.D.1    Melse-Boonstra, A.2    West, C.E.3    Van Breemen, R.B.4
  • 173
    • 0032401865 scopus 로고    scopus 로고
    • Determination of folate patterns in mouse plasma, erythrocytes, and embryos by HPLC coupled with a microbiological assay
    • S. Belz, and H. Nau Determination of folate patterns in mouse plasma, erythrocytes, and embryos by HPLC coupled with a microbiological assay Anal. Biochem. 265 1998 157 166
    • (1998) Anal. Biochem. , vol.265 , pp. 157-166
    • Belz, S.1    Nau, H.2
  • 174
    • 0021922416 scopus 로고
    • Endogenous folates of normal fibroblasts using high-performance liquid chromatography and modified extraction procedure
    • S.A. Kashani, and B.A. Cooper Endogenous folates of normal fibroblasts using high-performance liquid chromatography and modified extraction procedure Anal. Biochem. 146 1985 40 47
    • (1985) Anal. Biochem. , vol.146 , pp. 40-47
    • Kashani, S.A.1    Cooper, B.A.2
  • 175
    • 0022559147 scopus 로고
    • High-performance liquid chromatographic separation of the naturally occurring folic acid derivatives
    • S.D. Wilson, and D.W. Horne High-performance liquid chromatographic separation of the naturally occurring folic acid derivatives Methods Enzymol. 122 1986 269 273
    • (1986) Methods Enzymol. , vol.122 , pp. 269-273
    • Wilson, S.D.1    Horne, D.W.2
  • 176
    • 0021735886 scopus 로고
    • High-performance liquid chromatographic determination of the distribution of naturally occurring folic acid derivatives in rat liver
    • S.D. Wilson, and D.W. Horne High-performance liquid chromatographic determination of the distribution of naturally occurring folic acid derivatives in rat liver Anal. Biochem. 142 1984 529 535
    • (1984) Anal. Biochem. , vol.142 , pp. 529-535
    • Wilson, S.D.1    Horne, D.W.2
  • 177
    • 0023060679 scopus 로고
    • Microdetermination of folate monoglutamates in serum by liquid chromatography with electrochemical detection
    • M. Kohashi, K. Inoue, H. Sotobayashi, and K. Iwai Microdetermination of folate monoglutamates in serum by liquid chromatography with electrochemical detection J. Chromatogr. 382 1986 308 313
    • (1986) J. Chromatogr. , vol.382 , pp. 308-313
    • Kohashi, M.1    Inoue, K.2    Sotobayashi, H.3    Iwai, K.4
  • 178
    • 0037420731 scopus 로고    scopus 로고
    • Measurements of sub-nanomolar concentrations of unmetabolised folic acid in serum
    • M.R. Sweeney, J. McPartlin, D.G. Weir, and J.M. Scott Measurements of sub-nanomolar concentrations of unmetabolised folic acid in serum J. Chromatogr. B 788 2003 187 191
    • (2003) J. Chromatogr. B , vol.788 , pp. 187-191
    • Sweeney, M.R.1    McPartlin, J.2    Weir, D.G.3    Scott, J.M.4
  • 179
    • 0030200884 scopus 로고    scopus 로고
    • A combined high-performance liquid chromatographic-microbiological assay for serum folic acid
    • P. Kelly, J. McPartlin, and J. Scott A combined high-performance liquid chromatographic-microbiological assay for serum folic acid Anal. Biochem. 238 1996 179 183
    • (1996) Anal. Biochem. , vol.238 , pp. 179-183
    • Kelly, P.1    McPartlin, J.2    Scott, J.3
  • 180
    • 0030962568 scopus 로고    scopus 로고
    • Unmetabolized folic acid in serum: Acute studies in subjects consuming fortified food and supplements
    • P. Kelly, J. McPartlin, M. Goggins, D.G. Weir, and J.M. Scott Unmetabolized folic acid in serum: acute studies in subjects consuming fortified food and supplements Am. J. Clin. Nutr. 65 1997 1790 1795
    • (1997) Am. J. Clin. Nutr. , vol.65 , pp. 1790-1795
    • Kelly, P.1    McPartlin, J.2    Goggins, M.3    Weir, D.G.4    Scott, J.M.5
  • 181
    • 5844283052 scopus 로고
    • Multi-electrode array detectors in high-performance liquid chromatography: A new dimension in electrochemical analysis
    • C.N. Svendsen Multi-electrode array detectors in high-performance liquid chromatography: a new dimension in electrochemical analysis Analyst 118 1993 123 129
    • (1993) Analyst , vol.118 , pp. 123-129
    • Svendsen, C.N.1
  • 182
    • 0020520188 scopus 로고
    • High-performance liquid chromatographic separation of physiological folate monoglutamate compounds: Investigation of absorption and conversion of pteroylglutamic acid in the small intestine of the rat in situ
    • M. Tani, and K. Iwai High-performance liquid chromatographic separation of physiological folate monoglutamate compounds: investigation of absorption and conversion of pteroylglutamic acid in the small intestine of the rat in situ J. Chromatogr. 267 1983 175 181
    • (1983) J. Chromatogr. , vol.267 , pp. 175-181
    • Tani, M.1    Iwai, K.2
  • 183
    • 0035979757 scopus 로고    scopus 로고
    • Determination of folates in foods by high-performance liquid chromatography with fluorescence detection after precolumn conversion to 5-methyltetrahydrofolates
    • S. Ndaw, M. Bergaentzle, D. Aoude-Werner, S. Lahely, and C. Hasselmann Determination of folates in foods by high-performance liquid chromatography with fluorescence detection after precolumn conversion to 5-methyltetrahydrofolates J. Chromatogr. A 928 2001 77 90
    • (2001) J. Chromatogr. a , vol.928 , pp. 77-90
    • Ndaw, S.1    Bergaentzle, M.2    Aoude-Werner, D.3    Lahely, S.4    Hasselmann, C.5
  • 184
    • 0029049231 scopus 로고
    • Optimisation of chromatographic conditions for the determination of folates in foods and biological tissues for nutritional and clinical work
    • M.D. Lucock, M. Green, M. Priestnall, I. Daskalakis, M.I. Levene, and R. Hartley Optimisation of chromatographic conditions for the determination of folates in foods and biological tissues for nutritional and clinical work Food Chem. 53 1995 329 338
    • (1995) Food Chem. , vol.53 , pp. 329-338
    • Lucock, M.D.1    Green, M.2    Priestnall, M.3    Daskalakis, I.4    Levene, M.I.5    Hartley, R.6
  • 185
    • 0021323927 scopus 로고
    • Fluorometric determination of folacin in biological materials using high performance liquid chromatography
    • J.F. Gregory, D.B. Sartain, and B.P.F. Day Fluorometric determination of folacin in biological materials using high performance liquid chromatography J. Nutr. 114 1984 341 353
    • (1984) J. Nutr. , vol.114 , pp. 341-353
    • Gregory, J.F.1    Sartain, D.B.2    Day, B.P.F.3
  • 186
    • 0019548370 scopus 로고
    • Determination of folacin derivatives in selected foods by high performance liquid chromatography
    • B.P. Day, and J.F. Gregory Determination of folacin derivatives in selected foods by high performance liquid chromatography J. Agric. Food Chem. 29 1981 374 377
    • (1981) J. Agric. Food Chem. , vol.29 , pp. 374-377
    • Day, B.P.1    Gregory, J.F.2
  • 187
    • 0021323927 scopus 로고
    • Fluorometric determination of folacin in biological materials using high performance liquid chromatography
    • J.F. Gregory, D.S. Sartain, and B.P.F. Day Fluorometric determination of folacin in biological materials using high performance liquid chromatography J. Nutr. 114 1984 341 353
    • (1984) J. Nutr. , vol.114 , pp. 341-353
    • Gregory, J.F.1    Sartain, D.S.2    Day, B.P.F.3
  • 188
    • 0023475904 scopus 로고
    • Comparison of pterylpolyglutamate hydrolase (folate conjugase) from porcine and human intestinal brush border membrane
    • J.F. Gregory, S.L. Ink, and J.J. Cerda Comparison of pterylpolyglutamate hydrolase (folate conjugase) from porcine and human intestinal brush border membrane Comp. Biochem. Physiol. B 88 1987 1135 1141
    • (1987) Comp. Biochem. Physiol. B , vol.88 , pp. 1135-1141
    • Gregory, J.F.1    Ink, S.L.2    Cerda, J.J.3
  • 189
    • 84886606135 scopus 로고
    • Separation of substituted pteroyl monoglutamates and pteroyl oligo-γ-glutamates by high pressure liquid chromatography
    • R.W. Stout, A.R. Cashmore, J.K. Coward, C.G. Horvath, and J.R. Bertino Separation of substituted pteroyl monoglutamates and pteroyl oligo-γ-glutamates by high pressure liquid chromatography Anal. Biochem. 71 1976 119 124
    • (1976) Anal. Biochem. , vol.71 , pp. 119-124
    • Stout, R.W.1    Cashmore, A.R.2    Coward, J.K.3    Horvath, C.G.4    Bertino, J.R.5
  • 191
    • 15444375102 scopus 로고    scopus 로고
    • Capillary electrophoresis and high-performance liquid chromatography determination of polyglutamyl 5-methyltetrahydrofolate forms in citrus products
    • N.J. Matella, R.J. Braddock, J.F. Gregory, and R.M. Goodrich Capillary electrophoresis and high-performance liquid chromatography determination of polyglutamyl 5-methyltetrahydrofolate forms in citrus products J. Agric. Food. Chem. 53 2005 2268 2274
    • (2005) J. Agric. Food. Chem. , vol.53 , pp. 2268-2274
    • Matella, N.J.1    Braddock, R.J.2    Gregory, J.F.3    Goodrich, R.M.4
  • 192
    • 0029688186 scopus 로고    scopus 로고
    • Separation of methotrexate polyglutamates by capillary electrophoresis and its application to the measurement of γ-glutamyl hydrolase activity in human leukemia cells in culture
    • Y. Takemura, H. Kobayashi, and S. Sekiguchi Separation of methotrexate polyglutamates by capillary electrophoresis and its application to the measurement of γ-glutamyl hydrolase activity in human leukemia cells in culture Jpn. J. Clin. Pathol. 44 1996 51 56
    • (1996) Jpn. J. Clin. Pathol. , vol.44 , pp. 51-56
    • Takemura, Y.1    Kobayashi, H.2    Sekiguchi, S.3
  • 193
    • 0042920823 scopus 로고    scopus 로고
    • Combined marginal folate and riboflavin status affect homocysteine methylation in cultured immortalized lymphocytes from persons homozygous for the MTHFR C677T mutation
    • L. Lathrop Stern, B. Shane, P.J. Bagley, M. Nadeau, V. Shih, and J. Selhub Combined marginal folate and riboflavin status affect homocysteine methylation in cultured immortalized lymphocytes from persons homozygous for the MTHFR C677T mutation J. Nutr. 133 2003 2716 2720
    • (2003) J. Nutr. , vol.133 , pp. 2716-2720
    • Lathrop Stern, L.1    Shane, B.2    Bagley, P.J.3    Nadeau, M.4    Shih, V.5    Selhub, J.6
  • 195
    • 0022559151 scopus 로고
    • Tissue folate polyglutamate chain length determination by electrophoresis as thymidylate synthase-fluorodeoxyuridylate ternary complex
    • D.G. Priest, and M.T. Doig Tissue folate polyglutamate chain length determination by electrophoresis as thymidylate synthase-fluorodeoxyuridylate ternary complex Methods Enzymol. 122 1986 313 319
    • (1986) Methods Enzymol. , vol.122 , pp. 313-319
    • Priest, D.G.1    Doig, M.T.2
  • 196
    • 0019881451 scopus 로고
    • Tissue folylpolyglutamate chain length characterization by electrophoresis as thymidylate synthase-fluorodeoxyuridylate ternary complex
    • D.G. Priest, K.K. Happel, M. Magnum, J.M. Bednareck, M.T. Doig, and C.M. Baugh Tissue folylpolyglutamate chain length characterization by electrophoresis as thymidylate synthase-fluorodeoxyuridylate ternary complex Anal. Biochem. 115 1981 163 169
    • (1981) Anal. Biochem. , vol.115 , pp. 163-169
    • Priest, D.G.1    Happel, K.K.2    Magnum, M.3    Bednareck, J.M.4    Doig, M.T.5    Baugh, C.M.6
  • 198
    • 0017798863 scopus 로고
    • The oxidative cleavage of folates: A critical study
    • T. Marutama, T. Shiota, and C.L. Krumdieck The oxidative cleavage of folates: a critical study Anal. Biochem. 84 1978 277 295
    • (1978) Anal. Biochem. , vol.84 , pp. 277-295
    • Marutama, T.1    Shiota, T.2    Krumdieck, C.L.3
  • 199
    • 0019174565 scopus 로고
    • Cleavage of naturally occurring folates to unsubstituted p-aminobenzylpoly-γ-glutamates
    • S.K. Foo, D.J. Cichowicz, and B. Shane Cleavage of naturally occurring folates to unsubstituted p-aminobenzylpoly-γ-glutamates Anal. Biochem. 107 1980 109 115
    • (1980) Anal. Biochem. , vol.107 , pp. 109-115
    • Foo, S.K.1    Cichowicz, D.J.2    Shane, B.3
  • 200
    • 0019813887 scopus 로고
    • Determination of three different pools of reduced one-carbon-substituted folates: II. Quantitation and chain length determination of the pteroylpolyglutamates of rat liver
    • I. Eto, and C.L. Krumdiek Determination of three different pools of reduced one-carbon-substituted folates: II. Quantitation and chain length determination of the pteroylpolyglutamates of rat liver Anal. Biochem. 115 1981 138 146
    • (1981) Anal. Biochem. , vol.115 , pp. 138-146
    • Eto, I.1    Krumdiek, C.L.2
  • 201
    • 0022559146 scopus 로고
    • Identification of folylpoly(γ-glutamate) chain length by cleavage to and separation of p-aminobenzoylpoly(γ-glutamate)
    • B. Shane Identification of folylpoly(γ-glutamate) chain length by cleavage to and separation of p-aminobenzoylpoly(γ-glutamate) Methods Enzymol. 122 1986 323 331
    • (1986) Methods Enzymol. , vol.122 , pp. 323-331
    • Shane, B.1
  • 202
    • 0020472837 scopus 로고
    • Determination of three different pools of reduced one-carbon-substituted folates: III. Reversed-phase high-performance liquid chromatography of the azo-dye derivatives of p-aminobenzoylpoly-γ-glutamates and its application to the study of unlabeled endogenous pteroylpolyglutamates of rat liver
    • I. Eto, and C.L. Krumdieck Determination of three different pools of reduced one-carbon-substituted folates: III. Reversed-phase high-performance liquid chromatography of the azo-dye derivatives of p-aminobenzoylpoly-γ- glutamates and its application to the study of unlabeled endogenous pteroylpolyglutamates of rat liver Anal. Biochem. 120 1982 323 329
    • (1982) Anal. Biochem. , vol.120 , pp. 323-329
    • Eto, I.1    Krumdieck, C.L.2
  • 203
    • 0000139091 scopus 로고
    • A new coupling component for sulfanilamide determination
    • A.C. Bratton, and E.K. Marshall A new coupling component for sulfanilamide determination J. Biol. Chem. 128 1939 537 550
    • (1939) J. Biol. Chem. , vol.128 , pp. 537-550
    • Bratton, A.C.1    Marshall, E.K.2
  • 204
    • 0022559139 scopus 로고
    • Determination of p-aminobenzylpoly-γ-glutamates using fluorescamine
    • P.C. Loewen Determination of p-aminobenzylpoly-γ-glutamates using fluorescamine Methods Enzymol. 122 1986 330 333
    • (1986) Methods Enzymol. , vol.122 , pp. 330-333
    • Loewen, P.C.1
  • 205
    • 0029137557 scopus 로고
    • Synthesis of pteridines in Neurospora crassa, Phycomyces blakesleeanus, and Euglena gracilis: Detection and characterization of biosynthetic enzymes
    • J. Maier, and H. Hinnemann Synthesis of pteridines in Neurospora crassa, Phycomyces blakesleeanus, and Euglena gracilis: detection and characterization of biosynthetic enzymes Photochem. Photobiol. 61 1995 43 53
    • (1995) Photochem. Photobiol. , vol.61 , pp. 43-53
    • Maier, J.1    Hinnemann, H.2
  • 206
    • 1842645984 scopus 로고
    • Analysis of unconjugated pterins in food resources and human urine
    • M. Kohashi, K. Tomita, and K. Iwai Analysis of unconjugated pterins in food resources and human urine Agric. Biol. Chem. 44 1980 2089 2094
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 2089-2094
    • Kohashi, M.1    Tomita, K.2    Iwai, K.3
  • 207
    • 0019025468 scopus 로고
    • Isolation of six unconjugated pteridines from soybean (glycin max L. Tsurunoko) seeds
    • M. Kohashi Isolation of six unconjugated pteridines from soybean (glycin max L. Tsurunoko) seeds J. Biochem. 87 1980 1581 1586
    • (1980) J. Biochem. , vol.87 , pp. 1581-1586
    • Kohashi, M.1
  • 208
    • 0022559135 scopus 로고
    • Separation of pteridines from blood cells and plasma by reverse-phase high-performance liquid chromatography
    • H.-J. Zeitler, and B. Andondonskaja-Renz Separation of pteridines from blood cells and plasma by reverse-phase high-performance liquid chromatography Methods Enzymol. 122 1986 273 293
    • (1986) Methods Enzymol. , vol.122 , pp. 273-293
    • Zeitler, H.-J.1    Andondonskaja-Renz, B.2
  • 209
    • 0018868814 scopus 로고
    • Analysis of reduced forms of biopterin in biological tissues and fluids
    • T. Fukushima, and J.C. Nixon Analysis of reduced forms of biopterin in biological tissues and fluids Anal. Biochem. 102 1980 176 188
    • (1980) Anal. Biochem. , vol.102 , pp. 176-188
    • Fukushima, T.1    Nixon, J.C.2
  • 210
    • 0032227856 scopus 로고    scopus 로고
    • A sensitive assay for the enzymatic activity of GTP cyclohydrolase I
    • K. Hatakeyama, and T. Yoneyama A sensitive assay for the enzymatic activity of GTP cyclohydrolase I Methods Mol. Biol. 100 1998 265 272
    • (1998) Methods Mol. Biol. , vol.100 , pp. 265-272
    • Hatakeyama, K.1    Yoneyama, T.2
  • 211
    • 0021843863 scopus 로고
    • Pteridine formation during lectin-induced lymphocyte activation
    • I. Ziegler Pteridine formation during lectin-induced lymphocyte activation J. Cell. Biochem. 28 1985 197 206
    • (1985) J. Cell. Biochem. , vol.28 , pp. 197-206
    • Ziegler, I.1
  • 212
    • 0018886130 scopus 로고
    • Quantitative determination of pteridines in biological fluids by high-performance liquid chromatography
    • B. Stea, R.M. Halpern, B.C. Halpern, and R.S. Smith Quantitative determination of pteridines in biological fluids by high-performance liquid chromatography J. Chromatogr. 188 1980 363 375
    • (1980) J. Chromatogr. , vol.188 , pp. 363-375
    • Stea, B.1    Halpern, R.M.2    Halpern, B.C.3    Smith, R.S.4
  • 213
    • 0014027498 scopus 로고
    • Biosynthesis of pteridines and of phenylalanine hydroxylase cofactor in cell extracts of pseudomonas species (ATCC 11299a)
    • G. Guroff, and C.A. Strenkoski Biosynthesis of pteridines and of phenylalanine hydroxylase cofactor in cell extracts of pseudomonas species (ATCC 11299a) J. Biol. Chem. 241 1966 2220 2227
    • (1966) J. Biol. Chem. , vol.241 , pp. 2220-2227
    • Guroff, G.1    Strenkoski, C.A.2
  • 214
    • 0014409033 scopus 로고
    • The biosynthesis of folic acid: VIII. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate
    • A.W. Burg, and G.M. Brown The biosynthesis of folic acid: VIII. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate J. Biol. Chem. 243 1968 2349 2358
    • (1968) J. Biol. Chem. , vol.243 , pp. 2349-2358
    • Burg, A.W.1    Brown, G.M.2
  • 215
    • 0014939628 scopus 로고
    • The biosynthesis of folic acid: XI. Purification and properties of dihydroneopterin aldolase
    • J.B. Mathis, and G.M. Brown The biosynthesis of folic acid: XI. Purification and properties of dihydroneopterin aldolase J. Biol. Chem. 245 1970 3015 3025
    • (1970) J. Biol. Chem. , vol.245 , pp. 3015-3025
    • Mathis, J.B.1    Brown, G.M.2
  • 216
    • 0015240597 scopus 로고
    • Identification of the isomer of dihydroneopterin triphosphate synthesized by two enzyme fractions from Lactobacillus plantarum
    • R.J. Jackson, and T. Shiota Identification of the isomer of dihydroneopterin triphosphate synthesized by two enzyme fractions from Lactobacillus plantarum J. Biol. Chem. 246 1971 7454 7459
    • (1971) J. Biol. Chem. , vol.246 , pp. 7454-7459
    • Jackson, R.J.1    Shiota, T.2
  • 217
    • 0016366842 scopus 로고
    • The biosynthesis of folic acid: XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase
    • Y. Suzuki, and G.M. Brown The biosynthesis of folic acid: XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase J. Biol. Chem. 249 1974 2405 2410
    • (1974) J. Biol. Chem. , vol.249 , pp. 2405-2410
    • Suzuki, Y.1    Brown, G.M.2
  • 218
    • 0030872578 scopus 로고    scopus 로고
    • D-Erythro-neopterin biosynthesis in the methanogenic archaea Methanococcus thermophila and Methanobacterium thermoautotrophicum Δh
    • D.M. Howell, and R.H. White d-Erythro-neopterin biosynthesis in the methanogenic archaea Methanococcus thermophila and Methanobacterium thermoautotrophicum ΔH J. Bacteriol. 179 1997 5165 5170
    • (1997) J. Bacteriol. , vol.179 , pp. 5165-5170
    • Howell, D.M.1    White, R.H.2
  • 219
    • 0018797589 scopus 로고
    • Separation of unconjugated pteridines by high-pressure cation-exchange liquid chromatography
    • B. Stea, R.M. Halpern, and R.A. Smith Separation of unconjugated pteridines by high-pressure cation-exchange liquid chromatography J. Chromatogr. 168 1979 385 393
    • (1979) J. Chromatogr. , vol.168 , pp. 385-393
    • Stea, B.1    Halpern, R.M.2    Smith, R.A.3
  • 220
    • 0020601548 scopus 로고
    • Separation of pteridines from blood cells and plasma by reverse-phase high-performance liquid chromatography
    • B. Andondonskaja-Renz, and H.-J. Zeitler Separation of pteridines from blood cells and plasma by reverse-phase high-performance liquid chromatography Anal. Biochem. 133 1983 68 78
    • (1983) Anal. Biochem. , vol.133 , pp. 68-78
    • Andondonskaja-Renz, B.1    Zeitler, H.-J.2
  • 221
    • 0020570706 scopus 로고
    • The determination of pterins in biological samples by liquid chromatography/electrochemistry
    • C.E. Lunte, and P.T. Kissinger The determination of pterins in biological samples by liquid chromatography/electrochemistry Anal. Biochem. 129 1983 377 386
    • (1983) Anal. Biochem. , vol.129 , pp. 377-386
    • Lunte, C.E.1    Kissinger, P.T.2
  • 223
    • 0031725643 scopus 로고    scopus 로고
    • Characterization of mutants that allow p-aminobenzoyl-glutamate utilization by E. coli
    • M.J. Hussein, J.M. Green, and B.P. Nichols Characterization of mutants that allow p-aminobenzoyl-glutamate utilization by E. coli J. Bacteriol. 180 1998 6260 6268
    • (1998) J. Bacteriol. , vol.180 , pp. 6260-6268
    • Hussein, M.J.1    Green, J.M.2    Nichols, B.P.3
  • 224
    • 0025737957 scopus 로고
    • P-Aminobenzoate synthesis in Escherichia coli
    • J.M. Green, and B.P. Nichols p-Aminobenzoate synthesis in Escherichia coli J. Biol. Chem. 266 1991 12971 12975
    • (1991) J. Biol. Chem. , vol.266 , pp. 12971-12975
    • Green, J.M.1    Nichols, B.P.2
  • 226
    • 0024403436 scopus 로고
    • Para-Aminobenzoate synthesis from chorismate occurs in two steps
    • B.P. Nichols, A.M. Seibold, and S.Z. Dokor para-Aminobenzoate synthesis from chorismate occurs in two steps J. Biol. Chem. 264 1989 8597 8601
    • (1989) J. Biol. Chem. , vol.264 , pp. 8597-8601
    • Nichols, B.P.1    Seibold, A.M.2    Dokor, S.Z.3
  • 227
    • 0014803519 scopus 로고
    • Biosynthesis of 4-aminobenzoate in Escherichia coli
    • M. Huang, and F. Gibson Biosynthesis of 4-aminobenzoate in Escherichia coli J. Bacteriol. 103 1970 767 773
    • (1970) J. Bacteriol. , vol.103 , pp. 767-773
    • Huang, M.1    Gibson, F.2
  • 228
    • 0031692605 scopus 로고    scopus 로고
    • Biotransformation of p-aminobenzoic acid by cultured cells of Eucalyptus perriniana
    • T. Furuya, Y. Asada, S. Mizobata, Y. Matsuura, and H. Hamada Biotransformation of p-aminobenzoic acid by cultured cells of Eucalyptus perriniana Phytochemistry 49 1998 109 111
    • (1998) Phytochemistry , vol.49 , pp. 109-111
    • Furuya, T.1    Asada, Y.2    Mizobata, S.3    Matsuura, Y.4    Hamada, H.5
  • 229
    • 0033054231 scopus 로고    scopus 로고
    • Biotransformation of o- and p-aminobenzoic acids and N-acetyl p-aminobenzoic acid by cell suspension cultures of Solanum mammosum
    • A. Syahrani, E. Ratnasari, G. Indrayanto, and A.L. Wilkins Biotransformation of o- and p-aminobenzoic acids and N-acetyl p-aminobenzoic acid by cell suspension cultures of Solanum mammosum Phytochemistry 51 1999 615 620
    • (1999) Phytochemistry , vol.51 , pp. 615-620
    • Syahrani, A.1    Ratnasari, E.2    Indrayanto, G.3    Wilkins, A.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.