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Volumn 377, Issue 2, 2008, Pages 251-258

A comparison of sugar indicators enables a universal high-throughput sugar-1-phosphate nucleotidyltransferase assay

Author keywords

Carbohydrate; Enzyme; Glycosyltransferase; Nucleotide; Sugar

Indexed keywords

CARBOHYDRATES; ENZYMES; NUCLEOTIDES; PHOSPHATASES; SALMONELLA; SUGARS;

EID: 43049088411     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.03.018     Document Type: Article
Times cited : (68)

References (64)
  • 1
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • K. Ohtsubo J.D. Marth Glycosylation in cellular mechanisms of health and disease Cell 126 2006 855 867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 2
    • 0031127564 scopus 로고    scopus 로고
    • The role of carbohydrates in biologically active natural products
    • A.C. Weymouth-Wilson The role of carbohydrates in biologically active natural products Nat. Prod. Rep. 14 1997 99 110
    • (1997) Nat. Prod. Rep. , vol.14 , pp. 99-110
    • Weymouth-Wilson, A.C.1
  • 3
    • 3843086796 scopus 로고    scopus 로고
    • Genes and enzymes involved in deoxysugar biosynthesis in bacteria
    • A. Trefzer J.A. Salas A. Bechthold Genes and enzymes involved in deoxysugar biosynthesis in bacteria Nat. Prod. Rep. 16 1999 283 299
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 283-299
    • Trefzer, A.1    Salas, J.A.2    Bechthold, A.3
  • 4
    • 0032821706 scopus 로고    scopus 로고
    • Enzymatic synthesis of nucleotide sugars
    • T. Bulter L. Elling Enzymatic synthesis of nucleotide sugars Glycoconj. J. 16 1999 147 159
    • (1999) Glycoconj. J. , vol.16 , pp. 147-159
    • Bulter, T.1    Elling, L.2
  • 5
    • 25844442417 scopus 로고    scopus 로고
    • Altered glycan structures: The molecular basis of congenital disorders of glycosylation
    • H.H. Freeze M. Aebi Altered glycan structures: The molecular basis of congenital disorders of glycosylation Curr. Opin. Struct. Biol. 15 2005 490 498
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 490-498
    • Freeze, H.H.1    Aebi, M.2
  • 6
    • 33744523569 scopus 로고    scopus 로고
    • Enzymatic tools for engineering natural product glycosylation
    • S. Blanchard J.S. Thorson Enzymatic tools for engineering natural product glycosylation Curr. Opin. Chem. Biol. 10 2006 263 271
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 263-271
    • Blanchard, S.1    Thorson, J.S.2
  • 7
    • 0035022268 scopus 로고    scopus 로고
    • Nature’s carbohydrate chemists: The enzymatic glycosylation of bioactive bacterial metabolites
    • J.S. Thorson T.J. Hosted J.Q. Jiang J.B. Biggins J. Ahlert Nature’s carbohydrate chemists: The enzymatic glycosylation of bioactive bacterial metabolites Curr. Org. Chem. 5 2001 139 167
    • (2001) Curr. Org. Chem. , vol.5 , pp. 139-167
    • Thorson, J.S.1    Hosted, T.J.2    Jiang, J.Q.3    Biggins, J.B.4    Ahlert, J.5
  • 8
    • 34247626294 scopus 로고    scopus 로고
    • Unusual sugar biosynthesis and natural product glycodiversification
    • C.J. Thibodeaux C.E. Melancon H.W. Liu Unusual sugar biosynthesis and natural product glycodiversification Nature 446 2007 1008 1016
    • (2007) Nature , vol.446 , pp. 1008-1016
    • Thibodeaux, C.J.1    Melancon, C.E.2    Liu, H.W.3
  • 9
    • 0034872489 scopus 로고    scopus 로고
    • Glycosides in medicine: The role of glycosidic residue in biological activity
    • V. Kren L. Martinkova Glycosides in medicine: The role of glycosidic residue in biological activity Curr. Med. Chem. 8 2001 1303 1328
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1303-1328
    • Kren, V.1    Martinkova, L.2
  • 11
    • 0034671801 scopus 로고    scopus 로고
    • The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA)
    • W. Blankenfeldt M. Asuncion J.S. Lam J.H. Naismith The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA) EMBO J. 19 2000 6652 6663
    • (2000) EMBO J. , vol.19 , pp. 6652-6663
    • Blankenfeldt, W.1    Asuncion, M.2    Lam, J.S.3    Naismith, J.H.4
  • 13
    • 34547762178 scopus 로고    scopus 로고
    • Stereoselective synthesis of β-1-C-substituted 1,4-dideoxy-1,4-imino-d-galactitols and evaluation as UDP-galactopyranose mutase inhibitors
    • S. Desvergnes V. Desvergnes O.R. Martin K. Itoh H.W. Liu S. Py Stereoselective synthesis of β-1-C-substituted 1,4-dideoxy-1,4-imino-d-galactitols and evaluation as UDP-galactopyranose mutase inhibitors Bioorg. Med. Chem. 15 2007 6443 6449
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 6443-6449
    • Desvergnes, S.1    Desvergnes, V.2    Martin, O.R.3    Itoh, K.4    Liu, H.W.5    Py, S.6
  • 15
    • 0033053659 scopus 로고    scopus 로고
    • Synthesis and applications for unnatural sugar nucleotides
    • J.M. Elhalabi K.G. Rice Synthesis and applications for unnatural sugar nucleotides Curr. Med. Chem. 6 1999 93 116
    • (1999) Curr. Med. Chem. , vol.6 , pp. 93-116
    • Elhalabi, J.M.1    Rice, K.G.2
  • 16
    • 21244483529 scopus 로고    scopus 로고
    • Nucleotide deoxysugars: Essential tools for the glycosylation engineering of novel bioactive compounds
    • C. Rupprath T. Schumacher L. Elling Nucleotide deoxysugars: Essential tools for the glycosylation engineering of novel bioactive compounds Curr. Med. Chem. 12 2005 1637 1675
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1637-1675
    • Rupprath, C.1    Schumacher, T.2    Elling, L.3
  • 18
    • 37549017360 scopus 로고    scopus 로고
    • Hyaluronan synthases: A decade-plus of novel glycosyltransferases
    • P.H. Weigel P.L. Deangelis Hyaluronan synthases: A decade-plus of novel glycosyltransferases J. Biol. Chem. 282 2007 36777 36781
    • (2007) J. Biol. Chem. , vol.282 , pp. 36777-36781
    • Weigel, P.H.1    Deangelis, P.L.2
  • 19
    • 0026655074 scopus 로고
    • Enzyme-catalyzed oligosaccharide synthesis
    • Y. Ichikawa G.C. Look C.H. Wong Enzyme-catalyzed oligosaccharide synthesis Anal. Biochem. 202 1992 215 238
    • (1992) Anal. Biochem. , vol.202 , pp. 215-238
    • Ichikawa, Y.1    Look, G.C.2    Wong, C.H.3
  • 20
    • 0035203808 scopus 로고    scopus 로고
    • An HPLC method for the assay of UDP-glucose pyrophosphorylase and UDP-glucose-4-epimerase in Solieria chordalis (Rhodophyceae)
    • F. Goulard M. Diouris E. Deslandes J.Y. Floc’h An HPLC method for the assay of UDP-glucose pyrophosphorylase and UDP-glucose-4-epimerase in Solieria chordalis (Rhodophyceae) Phytochem. Anal. 12 2001 363 365
    • (2001) Phytochem. Anal. , vol.12 , pp. 363-365
    • Goulard, F.1    Diouris, M.2    Deslandes, E.3    Floc’h, J.Y.4
  • 21
    • 0344494024 scopus 로고    scopus 로고
    • An assay for adenosine 5′-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase
    • A. Yep C.M. Bejar M.A. Ballicora J.R. Dubay A.A. Iglesias J. Preiss An assay for adenosine 5′-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase Anal. Biochem. 324 2004 52 59
    • (2004) Anal. Biochem. , vol.324 , pp. 52-59
    • Yep, A.1    Bejar, C.M.2    Ballicora, M.A.3    Dubay, J.R.4    Iglesias, A.A.5    Preiss, J.6
  • 22
    • 0025802937 scopus 로고
    • A high-performance liquid chromatography-based radiometric assay for sucrose-phosphate synthase and other UDP-glucose requiring enzymes
    • M.E. Salvucci S.J. Crafts-Brandner A high-performance liquid chromatography-based radiometric assay for sucrose-phosphate synthase and other UDP-glucose requiring enzymes Anal. Biochem. 194 1991 365 368
    • (1991) Anal. Biochem. , vol.194 , pp. 365-368
    • Salvucci, M.E.1    Crafts-Brandner, S.J.2
  • 23
    • 0019867003 scopus 로고
    • A simplified radioactive assay for the enzyme UDP-glucose pyrophosphorylase
    • C.A. Evers C.M. Palatnik A simplified radioactive assay for the enzyme UDP-glucose pyrophosphorylase Anal. Biochem. 118 1981 108 112
    • (1981) Anal. Biochem. , vol.118 , pp. 108-112
    • Evers, C.A.1    Palatnik, C.M.2
  • 24
    • 0017074162 scopus 로고
    • An improved radiochemical assay for uridine diphosphoglucose pyrophosphorylase
    • B.D. Hames An improved radiochemical assay for uridine diphosphoglucose pyrophosphorylase Anal. Biochem. 73 1976 215 219
    • (1976) Anal. Biochem. , vol.73 , pp. 215-219
    • Hames, B.D.1
  • 25
    • 0029999425 scopus 로고    scopus 로고
    • An improved assay for UDP-glucose pyrophosphorylase and other enzymes that have nucleotide products
    • R.G. Duggleby H.L. Peng H.Y. Chang An improved assay for UDP-glucose pyrophosphorylase and other enzymes that have nucleotide products Experientia 52 1996 568 572
    • (1996) Experientia , vol.52 , pp. 568-572
    • Duggleby, R.G.1    Peng, H.L.2    Chang, H.Y.3
  • 26
    • 0030059624 scopus 로고    scopus 로고
    • A continuous microtiter plate assay for screening nucleotide sugar-synthesizing nucleotidyltransferases
    • J.E. Ritter C. Berlin L. Elling A continuous microtiter plate assay for screening nucleotide sugar-synthesizing nucleotidyltransferases Anal. Biochem. 234 1996 74 82
    • (1996) Anal. Biochem. , vol.234 , pp. 74-82
    • Ritter, J.E.1    Berlin, C.2    Elling, L.3
  • 27
    • 0030561461 scopus 로고    scopus 로고
    • A spectrophotometric method to measure enzymatic activity in reactions that generate inorganic pyrophosphate
    • R.H. Upson R.P. Haugland M.N. Malekzadeh A spectrophotometric method to measure enzymatic activity in reactions that generate inorganic pyrophosphate Anal. Biochem. 243 1996 41 45
    • (1996) Anal. Biochem. , vol.243 , pp. 41-45
    • Upson, R.H.1    Haugland, R.P.2    Malekzadeh, M.N.3
  • 28
    • 0033564278 scopus 로고    scopus 로고
    • A robotics-based automated assay for inorganic and organic phosphates
    • E.B. Cogan G.B. Birrell O.H. Griffith A robotics-based automated assay for inorganic and organic phosphates Anal. Biochem. 271 1999 29 35
    • (1999) Anal. Biochem. , vol.271 , pp. 29-35
    • Cogan, E.B.1    Birrell, G.B.2    Griffith, O.H.3
  • 30
    • 23044513080 scopus 로고    scopus 로고
    • Critical sources of error in colorimetric assay for UDP- N-acetylglucosamine pyrophosphorylase
    • M.T. Mok M.R. Edwards Critical sources of error in colorimetric assay for UDP- N -acetylglucosamine pyrophosphorylase Anal. Biochem. 343 2005 341 343
    • (2005) Anal. Biochem. , vol.343 , pp. 341-343
    • Mok, M.T.1    Edwards, M.R.2
  • 31
    • 2142817107 scopus 로고    scopus 로고
    • General assay for sugar nucleotidyltransferases using electrospray ionization mass spectrometry
    • C.J. Zea N.L. Pohl General assay for sugar nucleotidyltransferases using electrospray ionization mass spectrometry Anal. Biochem. 328 2004 196 202
    • (2004) Anal. Biochem. , vol.328 , pp. 196-202
    • Zea, C.J.1    Pohl, N.L.2
  • 33
    • 0345255629 scopus 로고    scopus 로고
    • Creation of the first anomeric d/l-sugar kinase by means of directed evolution
    • D. Hoffmeister J. Yang L. Liu J.S. Thorson Creation of the first anomeric d/l-sugar kinase by means of directed evolution Proc. Natl. Acad. Sci. USA 100 2003 13184 13189
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13184-13189
    • Hoffmeister, D.1    Yang, J.2    Liu, L.3    Thorson, J.S.4
  • 34
    • 4644229580 scopus 로고    scopus 로고
    • Structure-based enhancement of the first anomeric glucokinase
    • J. Yang L. Liu J.S. Thorson Structure-based enhancement of the first anomeric glucokinase ChemBioChem 5 2004 992 996
    • (2004) ChemBioChem , vol.5 , pp. 992-996
    • Yang, J.1    Liu, L.2    Thorson, J.S.3
  • 35
    • 4544373926 scopus 로고    scopus 로고
    • Mechanistic implications of Escherichia coli galactokinase structure-based engineering
    • D. Hoffmeister J.S. Thorson Mechanistic implications of Escherichia coli galactokinase structure-based engineering ChemBioChem 5 2004 989 992
    • (2004) ChemBioChem , vol.5 , pp. 989-992
    • Hoffmeister, D.1    Thorson, J.S.2
  • 36
    • 24944496018 scopus 로고    scopus 로고
    • Structure-based engineering of E. coli galactokinase as a first step toward in vivo glycorandomization
    • J. Yang X. Fu J. Liao L. Liu J.S. Thorson Structure-based engineering of E. coli galactokinase as a first step toward in vivo glycorandomization Chem. Biol. 12 2005 657 664
    • (2005) Chem. Biol. , vol.12 , pp. 657-664
    • Yang, J.1    Fu, X.2    Liao, J.3    Liu, L.4    Thorson, J.S.5
  • 37
    • 34447114483 scopus 로고    scopus 로고
    • Enhancing the latent nucleotide triphosphate flexibility of the glucose-1-phosphate thymidylyltransferase RmlA
    • R. Moretti J.S. Thorson Enhancing the latent nucleotide triphosphate flexibility of the glucose-1-phosphate thymidylyltransferase RmlA J. Biol. Chem. 282 2007 16942 16947
    • (2007) J. Biol. Chem. , vol.282 , pp. 16942-16947
    • Moretti, R.1    Thorson, J.S.2
  • 38
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • G.L. Miller Use of dinitrosalicylic acid reagent for determination of reducing sugar Anal. Chem. 31 1959 426 428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 39
    • 0022255318 scopus 로고
    • Determination of reducing sugars in the nanomole range with tetrazolium blue
    • C.K. Jue P.N. Lipke Determination of reducing sugars in the nanomole range with tetrazolium blue J. Biochem. Biophys. Methods 11 1985 109 115
    • (1985) J. Biochem. Biophys. Methods , vol.11 , pp. 109-115
    • Jue, C.K.1    Lipke, P.N.2
  • 40
    • 0019743542 scopus 로고
    • Modifications of the Park–Johnson ferricyanide submicromethod for the assay of reducing groups in carbohydrates
    • M. Porro S. Viti G. Antoni P. Neri Modifications of the Park–Johnson ferricyanide submicromethod for the assay of reducing groups in carbohydrates Anal. Biochem. 118 1981 301 306
    • (1981) Anal. Biochem. , vol.118 , pp. 301-306
    • Porro, M.1    Viti, S.2    Antoni, G.3    Neri, P.4
  • 41
    • 4244057586 scopus 로고
    • Determination of carbohydrates by condensation with 3-methyl-2-benzothiazolinone hydrazone
    • S. Honda Y. Nishimura H. Chiba K. Kakehi Determination of carbohydrates by condensation with 3-methyl-2-benzothiazolinone hydrazone Anal. Chim. Acta 131 1981 293 296
    • (1981) Anal. Chim. Acta , vol.131 , pp. 293-296
    • Honda, S.1    Nishimura, Y.2    Chiba, H.3    Kakehi, K.4
  • 42
    • 0037096082 scopus 로고    scopus 로고
    • Determination of reducing sugars with 3-methyl-2-benzothiazolinone hydrazone
    • G.E. Anthon D.M. Barrett Determination of reducing sugars with 3-methyl-2-benzothiazolinone hydrazone Anal. Biochem. 305 2002 287 289
    • (2002) Anal. Biochem. , vol.305 , pp. 287-289
    • Anthon, G.E.1    Barrett, D.M.2
  • 43
    • 0015333650 scopus 로고
    • A new reaction for colorimetric determination of carbohydrates
    • M. Lever A new reaction for colorimetric determination of carbohydrates Anal. Biochem. 47 1972 273 279
    • (1972) Anal. Biochem. , vol.47 , pp. 273-279
    • Lever, M.1
  • 45
    • 12944293659 scopus 로고
    • Mechanism of osazone formation
    • V.C. Barry P.W. Mitchell Mechanism of osazone formation Nature 175 1955 220
    • (1955) Nature , vol.175 , pp. 220
    • Barry, V.C.1    Mitchell, P.W.2
  • 46
    • 4243620067 scopus 로고
    • Mechanism in carbohydrate chemistry
    • B. Capon Mechanism in carbohydrate chemistry Chem. Rev. 69 1969 407 496
    • (1969) Chem. Rev. , vol.69 , pp. 407-496
    • Capon, B.1
  • 47
    • 0015914792 scopus 로고
    • Oxidation-reduction potential of the ferro-ferricyanide system in buffer solutions
    • J.E. O’Reilly Oxidation-reduction potential of the ferro-ferricyanide system in buffer solutions Biochim. Biophys. Acta 292 1973 509 515
    • (1973) Biochim. Biophys. Acta , vol.292 , pp. 509-515
    • O’Reilly, J.E.1
  • 48
    • 0000813694 scopus 로고
    • Preparation of a new tetrazolium salt which yields a blue pigment on reduction and its use in the demonstration of enzymes in normal and neoplastic tissues
    • A.M. Rutenburg R. Gofstein A.M. Seligman Preparation of a new tetrazolium salt which yields a blue pigment on reduction and its use in the demonstration of enzymes in normal and neoplastic tissues Cancer Res. 10 1950 113 121
    • (1950) Cancer Res. , vol.10 , pp. 113-121
    • Rutenburg, A.M.1    Gofstein, R.2    Seligman, A.M.3
  • 49
    • 85162688159 scopus 로고
    • UeberInvertseifen, VIII Mitteil: Reduktion von Tetrazoliumsalzen durch Bakterien, gaerende Hefe, und keimende Samen
    • R. Kuhn D. Jerchel UeberInvertseifen, VIII Mitteil: Reduktion von Tetrazoliumsalzen durch Bakterien, gaerende Hefe, und keimende Samen Ber. Deut. Chem. Ges. B 74 1941 949 952
    • (1941) Ber. Deut. Chem. Ges. B , vol.74 , pp. 949-952
    • Kuhn, R.1    Jerchel, D.2
  • 50
    • 3242727493 scopus 로고    scopus 로고
    • Green chemistry methods in sulfur dyeing: Application of various reducing D-sugars and analysis of the importance of optimum redox potential
    • R.S. Blackburn A. Harvey Green chemistry methods in sulfur dyeing: Application of various reducing D-sugars and analysis of the importance of optimum redox potential Environ. Sci. Technol. 38 2004 4034 4039
    • (2004) Environ. Sci. Technol. , vol.38 , pp. 4034-4039
    • Blackburn, R.S.1    Harvey, A.2
  • 51
    • 0014695116 scopus 로고
    • Anodic oxidation of carbohydrates and their derivatives in neutral saline solution
    • S.J. Yao A.J. Appleby A. Geisel H.R. Cash S.K. Wolfson Jr. Anodic oxidation of carbohydrates and their derivatives in neutral saline solution Nature 224 1969 921 922
    • (1969) Nature , vol.224 , pp. 921-922
    • Yao, S.J.1    Appleby, A.J.2    Geisel, A.3    Cash, H.R.4    Wolfson, S.K.5
  • 52
    • 0025766291 scopus 로고
    • Miniaturization of three carbohydrate analyses using a microsample plate reader
    • J.D. Fox J.F. Robyt Miniaturization of three carbohydrate analyses using a microsample plate reader Anal. Biochem. 195 1991 93 96
    • (1991) Anal. Biochem. , vol.195 , pp. 93-96
    • Fox, J.D.1    Robyt, J.F.2
  • 53
    • 0023406022 scopus 로고
    • Assay of reducing sugars in the nanomole range with 2,2′-bicinchoninate
    • S. Waffenschmidt L. Jaenicke Assay of reducing sugars in the nanomole range with 2,2′-bicinchoninate Anal. Biochem. 165 1987 337 340
    • (1987) Anal. Biochem. , vol.165 , pp. 337-340
    • Waffenschmidt, S.1    Jaenicke, L.2
  • 54
    • 0024452212 scopus 로고
    • Adaptation of the Nelson–Somogyi reducing-sugar assay to a microassay using microtiter plates
    • F. Green III C.A. Clausen T.L. Highley Adaptation of the Nelson–Somogyi reducing-sugar assay to a microassay using microtiter plates Anal. Biochem. 182 1989 197 199
    • (1989) Anal. Biochem. , vol.182 , pp. 197-199
    • Green, F.1    Clausen, C.A.2    Highley, T.L.3
  • 55
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • M. Somogyi Notes on sugar determination J. Biol. Chem. 195 1952 19 23
    • (1952) J. Biol. Chem. , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 56
    • 43049085240 scopus 로고
    • An evaluation of the alkaline para -hydroxybenzoic acid hydrazide procedure for the determination of reducing sugars
    • M.J. Koziol An evaluation of the alkaline para -hydroxybenzoic acid hydrazide procedure for the determination of reducing sugars Anal. Chim. Acta 128 1981 195 205
    • (1981) Anal. Chim. Acta , vol.128 , pp. 195-205
    • Koziol, M.J.1
  • 57
    • 0023931208 scopus 로고
    • Observations on the 4-hydroxybenzoylhydrazide methods for the determination of carbohydrates
    • I.M. Morrison E.H. Smith Observations on the 4-hydroxybenzoylhydrazide methods for the determination of carbohydrates Analyst 113 1988 841 842
    • (1988) Analyst , vol.113 , pp. 841-842
    • Morrison, I.M.1    Smith, E.H.2
  • 58
    • 0021240134 scopus 로고
    • Optimal conditions for 4-hydroxybenzoyl- and 2-furoylhydrazine as reagents for the determination of carbohydrates, including ketosamines
    • M. Lever T.A. Walmsley R.S. Visser S.J. Ryde Optimal conditions for 4-hydroxybenzoyl- and 2-furoylhydrazine as reagents for the determination of carbohydrates, including ketosamines Anal. Biochem. 139 1984 205 211
    • (1984) Anal. Biochem. , vol.139 , pp. 205-211
    • Lever, M.1    Walmsley, T.A.2    Visser, R.S.3    Ryde, S.J.4
  • 59
    • 0015609713 scopus 로고
    • Colorimetric and fluorometric carbohydrate determination with p-hydroxybenzoic acid hydrazide
    • M. Lever Colorimetric and fluorometric carbohydrate determination with p -hydroxybenzoic acid hydrazide Biochem. Med. 7 1973 274 281
    • (1973) Biochem. Med. , vol.7 , pp. 274-281
    • Lever, M.1
  • 60
    • 0015445672 scopus 로고
    • A new automated procedure for the colorimetric determination of glucose
    • J.C. Powell M. Lever A new automated procedure for the colorimetric determination of glucose Biochem. Med. 6 1972 543 547
    • (1972) Biochem. Med. , vol.6 , pp. 543-547
    • Powell, J.C.1    Lever, M.2
  • 61
    • 0015842839 scopus 로고
    • A comparison of 4-hydroxybenzoic acid hydrazide (PAHBAH) with other reagents for the determination of glucose
    • M. Lever J.C. Powell M. Killip C.W. Small A comparison of 4-hydroxybenzoic acid hydrazide (PAHBAH) with other reagents for the determination of glucose J. Lab. Clin. Med. 82 1973 649 655
    • (1973) J. Lab. Clin. Med. , vol.82 , pp. 649-655
    • Lever, M.1    Powell, J.C.2    Killip, M.3    Small, C.W.4
  • 62
    • 0017736277 scopus 로고
    • Carbohydrate determination with 4-hydroxybenzoic acid hydrazide (PAHBAH): Effect of bismuth on the reaction
    • M. Lever Carbohydrate determination with 4-hydroxybenzoic acid hydrazide (PAHBAH): Effect of bismuth on the reaction Anal. Biochem. 81 1977 21 27
    • (1977) Anal. Biochem. , vol.81 , pp. 21-27
    • Lever, M.1
  • 63
    • 0038756863 scopus 로고    scopus 로고
    • Potent inhibition of ribonuclease A by oligo(vinylsulfonic acid)
    • B.D. Smith M.B. Soellner R.T. Raines Potent inhibition of ribonuclease A by oligo(vinylsulfonic acid) J. Biol. Chem. 278 2003 20934 20938
    • (2003) J. Biol. Chem. , vol.278 , pp. 20934-20938
    • Smith, B.D.1    Soellner, M.B.2    Raines, R.T.3


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