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Volumn 143, Issue 2, 2006, Pages 249-255

Purification and kinetics of sheep kidney cortex glucose-6-phosphate dehydrogenase

Author keywords

Glucose 6 phosphate dehydrogenase; Kinetic mechanism; Optimum pH; Optimum temperature; Ping Pong Bi Bi system; Purification; Purification and aging

Indexed keywords

FREE RADICAL; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 31744446733     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2005.11.018     Document Type: Article
Times cited : (27)

References (53)
  • 1
    • 0034750551 scopus 로고    scopus 로고
    • Sex-linked differences in activity of enzymes in the blood of the urodele amphibian Pleurodeles waltl
    • T. Alekhova, A. Sof'in, T. Kobelkova, R. Marco, and C. Dournon Sex-linked differences in activity of enzymes in the blood of the urodele amphibian Pleurodeles waltl Comp. Biochem. Physiol. A 130 2001 819 825
    • (2001) Comp. Biochem. Physiol. a , vol.130 , pp. 819-825
    • Alekhova, T.1    Sof'In, A.2    Kobelkova, T.3    Marco, R.4    Dournon, C.5
  • 2
    • 0029114342 scopus 로고
    • Purification and characterization of Azotobacter vinelandii glucose-6-phosphate dehydrogenase: Dual coenzyme specificity
    • B.M. Anderson, and C.D. Anderson Purification and characterization of Azotobacter vinelandii glucose-6-phosphate dehydrogenase: dual coenzyme specificity Arch. Biochem. Biophys. 321 1995 94 100
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 94-100
    • Anderson, B.M.1    Anderson, C.D.2
  • 3
    • 0030320748 scopus 로고    scopus 로고
    • Regulation and properties of purified glucose-6-phosphate dehydrogenase from rat brain
    • M.A. Askar, K. Sumathy, and N.Z. Baquer Regulation and properties of purified glucose-6-phosphate dehydrogenase from rat brain Indian J. Biochem. Biophys. 33 1996 512 518
    • (1996) Indian J. Biochem. Biophys. , vol.33 , pp. 512-518
    • Askar, M.A.1    Sumathy, K.2    Baquer, N.Z.3
  • 4
    • 0026551994 scopus 로고
    • Purification and properties of human glucose-6-phosphate dehydrogenase made in Escherichia coli
    • J.M. Bautista, P.J. Mason, and L. Luzatto Purification and properties of human glucose-6-phosphate dehydrogenase made in Escherichia coli Biochim. Biophys. Acta 1119 1992 74 80
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 74-80
    • Bautista, J.M.1    Mason, P.J.2    Luzatto, L.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0033372008 scopus 로고    scopus 로고
    • Activity and metabolic roles of the pentose phosphate cycle in several rat tissues
    • H. Cabezas, R.R. Raposa, and E.M. Hevia Activity and metabolic roles of the pentose phosphate cycle in several rat tissues Mol. Cell. Biochem. 201 1-2 1999 57 63
    • (1999) Mol. Cell. Biochem. , vol.201 , Issue.1-2 , pp. 57-63
    • Cabezas, H.1    Raposa, R.R.2    Hevia, E.M.3
  • 8
    • 0017672621 scopus 로고
    • Characterization of the fatty acid-sensitive glucose 6-phosphate dehydrogenase from Pseudomonas cepacia
    • A.F Cacciapuoti, and T.G. Lessie Characterization of the fatty acid-sensitive glucose 6-phosphate dehydrogenase from Pseudomonas cepacia J. Bacteriol. 132 2 1977 555 563
    • (1977) J. Bacteriol. , vol.132 , Issue.2 , pp. 555-563
    • Cacciapuoti, A.F.1    Lessie, T.G.2
  • 9
    • 0031406893 scopus 로고    scopus 로고
    • Enzymes in Antarctic fish: Glucose-6-phosphate dehydrogenase and glutamate dehydrogenase
    • M.A. Ciardiello, L. Camardella, V. Carratore, and G. di Prisco Enzymes in Antarctic fish: glucose-6-phosphate dehydrogenase and glutamate dehydrogenase Comp. Biochem. Physiol. A 118 1997 1031 1036
    • (1997) Comp. Biochem. Physiol. a , vol.118 , pp. 1031-1036
    • Ciardiello, M.A.1    Camardella, L.2    Carratore, V.3    Di Prisco, G.4
  • 10
    • 0028924755 scopus 로고
    • Kinetic properties of hexose-monophosphate dehydrogenases: I. Isolation and partial purification of glucose-6-phosphate dehydrogenase from rat liver and kidney cortex
    • F.J. Corpas, L. Garcia-Salguero, J. Peragon, and J.A. Lupianez Kinetic properties of hexose-monophosphate dehydrogenases: I. Isolation and partial purification of glucose-6-phosphate dehydrogenase from rat liver and kidney cortex Life Sci. 56 1995 179 189
    • (1995) Life Sci. , vol.56 , pp. 179-189
    • Corpas, F.J.1    Garcia-Salguero, L.2    Peragon, J.3    Lupianez, J.A.4
  • 12
    • 0035078010 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase in barley roots: Kinetic properties and localisation of the isoforms
    • S. Esposito, S. Carfagna, G. Massaro, V. Vona, and V Di Martino Rigano Glucose-6-phosphate dehydrogenase in barley roots: kinetic properties and localisation of the isoforms Planta 212 2001 627 634
    • (2001) Planta , vol.212 , pp. 627-634
    • Esposito, S.1    Carfagna, S.2    Massaro, G.3    Vona, V.4    M.rigano, D.V.5
  • 13
    • 0030588315 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase from the Cyanobacterium, anabaena sp. PCC 7120: Purification and kinetics of redox modulation
    • F.K. Gleason Glucose-6-phosphate dehydrogenase from the Cyanobacterium, anabaena sp. PCC 7120: purification and kinetics of redox modulation Arch. Biochem. Biophys. 334 1996 277 283
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 277-283
    • Gleason, F.K.1
  • 14
    • 0037027540 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: Expression of the g6pd gene and characterization of an extremely thermophilic enzyme
    • T. Hansen, B. Schlichting, and P. Schonheit Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: expression of the g6pd gene and characterization of an extremely thermophilic enzyme FEMS Microbiol. Lett. 216 2 2002 249 253
    • (2002) FEMS Microbiol. Lett. , vol.216 , Issue.2 , pp. 249-253
    • Hansen, T.1    Schlichting, B.2    Schonheit, P.3
  • 15
    • 0020713197 scopus 로고
    • Tandem dye-ligand chromatography and biospecific elution applied to the purification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides
    • Y. Hey, and P.D. Dean Tandem dye-ligand chromatography and biospecific elution applied to the purification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides Biochem. J. 209 1983 363 371
    • (1983) Biochem. J. , vol.209 , pp. 363-371
    • Hey, Y.1    Dean, P.D.2
  • 16
    • 0036691498 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of the gsdA gene encoding thermophilic glucose-6-phosphate dehydrogenase from Aquifex aeolicus
    • R.B. Iyer, J. Wang, and L.G. Bachas Cloning, expression, and characterization of the gsdA gene encoding thermophilic glucose-6-phosphate dehydrogenase from Aquifex aeolicus Extremophiles 6 2002 283 289
    • (2002) Extremophiles , vol.6 , pp. 283-289
    • Iyer, R.B.1    Wang, J.2    Bachas, L.G.3
  • 17
    • 0031415638 scopus 로고    scopus 로고
    • Effect of temperature on the activities of glucose-6-phosphate dehydrogenase and hexokinase in entomopathogenic nematodes (Nematoda: Steinernematidae)
    • G.B. Jagdale, and R. Gordon Effect of temperature on the activities of glucose-6-phosphate dehydrogenase and hexokinase in entomopathogenic nematodes (Nematoda: Steinernematidae) Comp. Biochem. Physiol. A 118 1997 1151 1156
    • (1997) Comp. Biochem. Physiol. a , vol.118 , pp. 1151-1156
    • Jagdale, G.B.1    Gordon, R.2
  • 19
    • 0023667361 scopus 로고
    • Affinity partitioning of enzymes using dextran-bound procion yellow HE-3G. Influence of dye-ligand density
    • G. Johansson, and J. Joelsson Affinity partitioning of enzymes using dextran-bound procion yellow HE-3G. Influence of dye-ligand density J. Chromatogr. 393 1987 195 208
    • (1987) J. Chromatogr. , vol.393 , pp. 195-208
    • Johansson, G.1    Joelsson, J.2
  • 20
    • 0017065935 scopus 로고
    • Glucose-6-phosphate dehydrogenase. Purification and partial characterization
    • M.I. Kanji, M.L. Toews, and W.R. Carper Glucose-6-phosphate dehydrogenase. Purification and partial characterization J. Biol. Chem. 251 1976 2255 2257
    • (1976) J. Biol. Chem. , vol.251 , pp. 2255-2257
    • Kanji, M.I.1    Toews, M.L.2    Carper, W.R.3
  • 21
    • 10344221577 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency: A hidden risk for kernicterus
    • M. Kaplan, and C. Hammerman Glucose-6-phosphate dehydrogenase deficiency: a hidden risk for kernicterus Semin. Perinatol. 28 2004 356 364
    • (2004) Semin. Perinatol. , vol.28 , pp. 356-364
    • Kaplan, M.1    Hammerman, C.2
  • 23
    • 0022039273 scopus 로고
    • Glucose-6-phosphate dehydrogenase in normal human thrombocytes and in ischemic heart disease
    • G.V. Kudriavtseva, S.A. Makarov, and L.V. Shatalina Glucose-6-phosphate dehydrogenase in normal human thrombocytes and in ischemic heart disease Vopr. Med. Khim. 31 1985 90 94
    • (1985) Vopr. Med. Khim. , vol.31 , pp. 90-94
    • Kudriavtseva, G.V.1    Makarov, S.A.2    Shatalina, L.V.3
  • 24
    • 0018795536 scopus 로고
    • Purification and characterization of mouse glucose 6-phosphate dehydrogenase
    • C.Y. Lee, J.H. Yuan, D. Moser, and J.M. Kramer Purification and characterization of mouse glucose 6-phosphate dehydrogenase Mol. Cell Biochem. 24 1979 67 73
    • (1979) Mol. Cell Biochem. , vol.24 , pp. 67-73
    • Lee, C.Y.1    Yuan, J.H.2    Moser, D.3    Kramer, J.M.4
  • 25
    • 0018296923 scopus 로고
    • Glucose-6-phosphate dehydrogenases
    • A. Meister John Wiley and Sons Inc. New York
    • H.R. Levy Glucose-6-phosphate dehydrogenases A. Meister Advan. Enzymol. vol. 48 1979 John Wiley and Sons Inc. New York 97 191
    • (1979) Advan. Enzymol. , vol.48 , pp. 97-191
    • Levy, H.R.1
  • 26
    • 0025885775 scopus 로고
    • Purification and properties of NADP-linked glucose-6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum)
    • H.R. Levy, and C. Cook Purification and properties of NADP-linked glucose-6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum) Arch. Biochem. Biophys. 291 1991 161 167
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 161-167
    • Levy, H.R.1    Cook, C.2
  • 27
    • 31744444374 scopus 로고
    • Glucose-6-phosphate dehydrogenase from L. mesenteroides: Revised kinetic mechanism and kinetics of ATP inhibition
    • H.R. Levy, M. Christoff, and J. Ingulli Glucose-6-phosphate dehydrogenase from L. mesenteroides: revised kinetic mechanism and kinetics of ATP inhibition Arch. Biochem. Biophys. 26 1983 195 200
    • (1983) Arch. Biochem. Biophys. , vol.26 , pp. 195-200
    • Levy, H.R.1    Christoff, M.2    Ingulli, J.3
  • 29
    • 31744450479 scopus 로고
    • Purification of glucose 6-phosphate dehydrogenase from the sea-urchin, Hemicentrotus pulcherrimus
    • N. Matsuoka Purification of glucose 6-phosphate dehydrogenase from the sea-urchin, Hemicentrotus pulcherrimus Comp. Biochem. Physiol. B 89 1988 517 520
    • (1988) Comp. Biochem. Physiol. B , vol.89 , pp. 517-520
    • Matsuoka, N.1
  • 30
    • 0033946341 scopus 로고    scopus 로고
    • Kinetic properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo
    • B. Moritz, K. Striegel, A.A. De Graaf, and H. Sahm Kinetic properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo Eur. J. Biochem. 267 2000 3442 3452
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3442-3452
    • Moritz, B.1    Striegel, K.2    De Graaf, A.A.3    Sahm, H.4
  • 31
    • 0027225636 scopus 로고
    • Isolation and the complete amino acid sequence of lumenal endoplasmic reticulum glucose-6-phosphate dehydrogenase
    • J. Ozols Isolation and the complete amino acid sequence of lumenal endoplasmic reticulum glucose-6-phosphate dehydrogenase Proc. Natl. Acad. Sci. U. S. A. 90 1993 5302 5306
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 5302-5306
    • Ozols, J.1
  • 32
    • 0016417591 scopus 로고
    • 6-Phosphogluconate dehydrogenase from human erythrocytes
    • B.M.F. Pearse, and M.A. Rosemeyer 6-Phosphogluconate dehydrogenase from human erythrocytes Methods Enzymol. 41 1975 220 226
    • (1975) Methods Enzymol. , vol.41 , pp. 220-226
    • Pearse, B.M.F.1    Rosemeyer, M.A.2
  • 33
    • 0026595622 scopus 로고
    • Rapid isolation of glucose-6-phosphate dehydrogenase from human erythrocytes by combined affinity and anion-exchange chromatography for biochemical characterization of variants
    • S. Pittalis, F.M. Montemuros, D. Tavazzi, and G. Fiorelli Rapid isolation of glucose-6-phosphate dehydrogenase from human erythrocytes by combined affinity and anion-exchange chromatography for biochemical characterization of variants J. Chromatogr.: Biomed. Applic. 573 1992 29 34
    • (1992) J. Chromatogr.: Biomed. Applic. , vol.573 , pp. 29-34
    • Pittalis, S.1    Montemuros, F.M.2    Tavazzi, D.3    Fiorelli, G.4
  • 34
    • 0037457697 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase partitioning in two-phase aqueous mixed (nonionic/cationic) micellar systems
    • C.O. Rangel-Yagui, H. Lam, D.T. Kamei, D.I. Wang, A. Pessoa Jr., and D. Blankschtein Glucose-6-phosphate dehydrogenase partitioning in two-phase aqueous mixed (nonionic/cationic) micellar systems Biotechnol. Bioeng. 82 2003 445 456
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 445-456
    • Rangel-Yagui, C.O.1    Lam, H.2    Kamei, D.T.3    Wang, D.I.4    Pessoa Jr., A.5    Blankschtein, D.6
  • 35
    • 0025093333 scopus 로고
    • Purification and characterization of glucose-6-phosphate dehydrogenase from Pseudomonas W6
    • R. Reuter, M. Naumann, P. Metz, and G. Kopperschlager Purification and characterization of glucose-6-phosphate dehydrogenase from Pseudomonas W6 Biomed. Biochim. Acta. 49 1990 539 546
    • (1990) Biomed. Biochim. Acta. , vol.49 , pp. 539-546
    • Reuter, R.1    Naumann, M.2    Metz, P.3    Kopperschlager, G.4
  • 36
    • 0015240273 scopus 로고
    • Purification and partial characterization of glucose 6-phosphate dehydrogenase from Neurospora crassa
    • W.A. Scott, and E.L. Tatum Purification and partial characterization of glucose 6-phosphate dehydrogenase from Neurospora crassa J. Biol. Chem. 246 1971 6347 6352
    • (1971) J. Biol. Chem. , vol.246 , pp. 6347-6352
    • Scott, W.A.1    Tatum, E.L.2
  • 37
    • 0003518480 scopus 로고
    • 3rd ed. John Wiley and Sons Toronto
    • I.H. Segel Enzyme Kinetics 3rd ed. 1975 John Wiley and Sons Toronto 273 Chapter 9 and 11
    • (1975) Enzyme Kinetics , pp. 273
    • Segel, I.H.1
  • 38
    • 0027328852 scopus 로고
    • Protein oxidative damage is associated with life expectancy of houseflies
    • R.S. Sohal, S. Agarwal, A. Dubey, and W.C. Orr Protein oxidative damage is associated with life expectancy of houseflies Proc. Natl. Acad. Sci. U. S. A. 90 1993 7255 7259
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 7255-7259
    • Sohal, R.S.1    Agarwal, S.2    Dubey, A.3    Orr, W.C.4
  • 39
    • 0023682912 scopus 로고
    • Biochemical markers of aging
    • E.R. Stadtman Biochemical markers of aging Exp. Gerontol. 23 1988 327 347
    • (1988) Exp. Gerontol. , vol.23 , pp. 327-347
    • Stadtman, E.R.1
  • 41
    • 31744450045 scopus 로고    scopus 로고
    • Characterization of glucose-6-phosphate dehydrogenase purified from lamb kidney cortex Turk
    • B. Tandogan, and N.N. Ulusu Characterization of glucose-6-phosphate dehydrogenase purified from lamb kidney cortex Turk J. Biochem. 30 2005 178 182
    • (2005) J. Biochem. , vol.30 , pp. 178-182
    • Tandogan, B.1    Ulusu, N.N.2
  • 42
    • 0031909446 scopus 로고    scopus 로고
    • Purification of guinea pig small intestinal peroxisomes and the subcellular localization of glucose-6-phosphate dehydrogenase
    • P.S. Tappia, C.J. Jones, and M.J. Connock Purification of guinea pig small intestinal peroxisomes and the subcellular localization of glucose-6-phosphate dehydrogenase Mol. Cell Biochem. 179 1998 13 20
    • (1998) Mol. Cell Biochem. , vol.179 , pp. 13-20
    • Tappia, P.S.1    Jones, C.J.2    Connock, M.J.3
  • 45
    • 0348048778 scopus 로고    scopus 로고
    • Sex-specific metabolic changes in the annual reproductive cycle of a freshwater catfish
    • G. Tripathi, and P. Verma Sex-specific metabolic changes in the annual reproductive cycle of a freshwater catfish Comp. Biochem. Physiol. B 137 2004 101 106
    • (2004) Comp. Biochem. Physiol. B , vol.137 , pp. 101-106
    • Tripathi, G.1    Verma, P.2
  • 46
    • 0032458781 scopus 로고    scopus 로고
    • Purification and kinetic characterization of hexokinase and glucose-6-phosphate dehydrogenase from Schizosaccharomyces pombe
    • C.S. Tsai, and Q. Chen Purification and kinetic characterization of hexokinase and glucose-6-phosphate dehydrogenase from Schizosaccharomyces pombe Biochem. Cell Biol. 76 1998 107 113
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 107-113
    • Tsai, C.S.1    Chen, Q.2
  • 47
    • 0032810627 scopus 로고    scopus 로고
    • A rapid method for the purification of glucose-6-phosphate dehydrogenase from bovine lens
    • N.N. Ulusu, M.S. Kus, N.L. Acan, and E.F. Tezcan A rapid method for the purification of glucose-6-phosphate dehydrogenase from bovine lens Int. J. Biochem. Cell Biol. 31 1999 787 796
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 787-796
    • Ulusu, N.N.1    Kus, M.S.2    Acan, N.L.3    Tezcan, E.F.4
  • 48
    • 14844330087 scopus 로고    scopus 로고
    • Kinetic properties of glucose-6-phosphate dehydrogenase from lamb kidney cortex
    • N.N. Ulusu, B. Tandogan, and E.F. Tezcan Kinetic properties of glucose-6-phosphate dehydrogenase from lamb kidney cortex Biochimie 87 2005 187 190
    • (2005) Biochimie , vol.87 , pp. 187-190
    • Ulusu, N.N.1    Tandogan, B.2    Tezcan, E.F.3
  • 49
    • 0042838106 scopus 로고    scopus 로고
    • Glutathione and catalase provide overlapping defenses for protection against respiration-generated hydrogen peroxide in Haemophilus influenzae
    • B. Vergauwen, F. Pauwels, and J.J. Van Beeumen Glutathione and catalase provide overlapping defenses for protection against respiration-generated hydrogen peroxide in Haemophilus influenzae J. Bacteriol. 185 18 2003 5555 5562
    • (2003) J. Bacteriol. , vol.185 , Issue.18 , pp. 5555-5562
    • Vergauwen, B.1    Pauwels, F.2    Van Beeumen, J.J.3
  • 50
    • 9244245288 scopus 로고    scopus 로고
    • Glucose 6-phosphate dehydrogenase deficiency: A protection against malaria and a risk for hemolytic accidents
    • H. Wajcman, and F. Galacteros Glucose 6-phosphate dehydrogenase deficiency: a protection against malaria and a risk for hemolytic accidents C.R. Biol. 327 2004 711 720
    • (2004) C.R. Biol. , vol.327 , pp. 711-720
    • Wajcman, H.1    Galacteros, F.2
  • 51
    • 0027332210 scopus 로고
    • Purification and characterization of glucose-6-phosphate dehydrogenase from Aspergillus niger and Aspergillus nidulans
    • L.M. Wennekes, T. Goosen, P.J. van den Broek, and H.W. van den Broek Purification and characterization of glucose-6-phosphate dehydrogenase from Aspergillus niger and Aspergillus nidulans Gen. Microbiol. 139 1993 2793 2800
    • (1993) Gen. Microbiol. , vol.139 , pp. 2793-2800
    • Wennekes, L.M.1    Goosen, T.2    Van Den Broek, P.J.3    Van Den Broek, H.W.4
  • 52
    • 0038481114 scopus 로고    scopus 로고
    • Relationship between gluconeogenesis and glutathione redox state in rabbit kidney-cortex tubules
    • K. Winiarska, J. Drozak, M. Wegrzynowicz, A.K. Jagielski, and J. Bryla Relationship between gluconeogenesis and glutathione redox state in rabbit kidney-cortex tubules Metabolism 52 2003 739 746
    • (2003) Metabolism , vol.52 , pp. 739-746
    • Winiarska, K.1    Drozak, J.2    Wegrzynowicz, M.3    Jagielski, A.K.4    Bryla, J.5
  • 53
    • 0036375584 scopus 로고    scopus 로고
    • Recombinant human glucose-6-phosphate dehydrogenase. Evidence for a rapid equilibrium random-ordered mechanism
    • X.T. Wang, S.W. Au, V.M. Lam, and P.C. Engel Recombinant human glucose-6-phosphate dehydrogenase. Evidence for a rapid equilibrium random-ordered mechanism Eur. J. Biochem. 269 2002 3417 3424
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3417-3424
    • Wang, X.T.1    Au, S.W.2    Lam, V.M.3    Engel, P.C.4


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