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Volumn 87, Issue 2, 2005, Pages 187-190

Kinetic properties of glucose-6-phosphate dehydrogenase from lamb kidney cortex

Author keywords

Glucose 6 phosphate dehydrogenase; Kinetics; Lamb kidney cortex

Indexed keywords

2 DIETHYLAMINOETHANOL; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; SEPHAROSE;

EID: 14844330087     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.11.002     Document Type: Article
Times cited : (23)

References (24)
  • 1
    • 0018296923 scopus 로고
    • Glucose-6-phosphate dehydrogenases
    • A. Meister John Wiley and Sons New York
    • H.R. Levy Glucose-6-phosphate dehydrogenases A. Meister Advances in Enzymology, vol. 48 1979 John Wiley and Sons New York 97 192
    • (1979) Advances in Enzymology, Vol. 48 , pp. 97-192
    • Levy, H.R.1
  • 2
    • 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. Melendez-Hevia Activity and metabolic roles of the pentose phosphate cycle in several rat tissues Mol. Cell. Biochem. 201 1999 57 63
    • (1999) Mol. Cell. Biochem. , vol.201 , pp. 57-63
    • Cabezas, H.1    Raposa, R.R.2    Melendez-Hevia, E.3
  • 3
    • 0033957465 scopus 로고    scopus 로고
    • The effect of selenium on glutathione redox cycle enzymes of some rabbit tissues
    • N.N. Ulusu, N.L. Acan, B. Turan, and E.F. Tezcan The effect of selenium on glutathione redox cycle enzymes of some rabbit tissues Trace Elements and Electrolytes 17 2000 25 29
    • (2000) Trace Elements and Electrolytes , vol.17 , pp. 25-29
    • Ulusu, N.N.1    Acan, N.L.2    Turan, B.3    Tezcan, E.F.4
  • 6
    • 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
  • 7
    • 0027399842 scopus 로고
    • Study of glucose-6 phosphate dehydrogenase: History and molecular biology
    • E. Beutler Study of glucose-6 phosphate dehydrogenase: history and molecular biology Am. J. Hematol. 42 1993 53 58
    • (1993) Am. J. Hematol. , vol.42 , pp. 53-58
    • Beutler, E.1
  • 8
    • 0028279664 scopus 로고
    • +-preferring glucose-6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum)
    • +-preferring glucose-6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum) Arch. Biochem. Biophys. 310 1994 360 366
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 360-366
    • Ragunathan, S.1    Levy, H.R.2
  • 9
    • 0036700420 scopus 로고    scopus 로고
    • Purification and characterization of glucose-6-phosphate dehydrogenase from sheep erythrocytes and inhibitory effects of some antibiotics on enzyme activity
    • S. Beydemir, M. Ciftci, and O.I. Kufrevioglu Purification and characterization of glucose-6-phosphate dehydrogenase from sheep erythrocytes and inhibitory effects of some antibiotics on enzyme activity Journal of Enzyme Inhibition and Medicinal Chemistry 17 2002 271 277
    • (2002) Journal of Enzyme Inhibition and Medicinal Chemistry , vol.17 , pp. 271-277
    • Beydemir, S.1    Ciftci, M.2    Kufrevioglu, O.I.3
  • 12
    • 0016417591 scopus 로고
    • 6-Phosphogluconate Dehydrogenase from human erythrocytes
    • S.R. Colowich N.O. Kaplan Academic Press Inc.
    • B.M.F. Pearse, and M.A. Rosemeyer 6-Phosphogluconate Dehydrogenase from human erythrocytes S.R. Colowich N.O. Kaplan Methods in Enzymology, vol. 41 1975 Academic Press Inc. 220 226
    • (1975) Methods in Enzymology, Vol. 41 , pp. 220-226
    • Pearse, B.M.F.1    Rosemeyer, M.A.2
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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.G. 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.G.2    Peragon, J.3    Lupianez, J.A.4
  • 16
    • 0020440235 scopus 로고
    • Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models
    • S.P. Colowick N.O. Kaplan Academic Press Inc Orlando
    • B. Mannervik Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models S.P. Colowick N.O. Kaplan Methods in Enzymology, vol. 87 1982 Academic Press Inc Orlando 370 390
    • (1982) Methods in Enzymology, Vol. 87 , pp. 370-390
    • Mannervik, B.1
  • 18
    • 0026094986 scopus 로고
    • Kinetic properties of normal human erythrocyte glucose-6-phosphate dehydrogenase dimmers
    • S.A. Adediran Kinetic properties of normal human erythrocyte glucose-6-phosphate dehydrogenase dimmers Biochimie 73 1991 1211 1218
    • (1991) Biochimie , vol.73 , pp. 1211-1218
    • Adediran, S.A.1
  • 19
    • 0033946341 scopus 로고    scopus 로고
    • Kinetic properties of the glucose-6-phosphate dehydrogenase from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo
    • B. Moritz, K. Striegel, A.A. DeGraaf, and H. Sahm Kinetic properties of the glucose-6-phosphate dehydrogenase 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    Degraaf, A.A.3    Sahm, H.4
  • 20
    • 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
  • 21
    • 0021103822 scopus 로고
    • Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: Revised kinetic mechanism and kinetics of ATP inhibition
    • H.R. Levy, M. Christoff, J. Ingulli, and E.M. Ho Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: revised kinetic mechanism and kinetics of ATP inhibition Arch. Biochem. Biophys. 222 1983 473 478
    • (1983) Arch. Biochem. Biophys. , vol.222 , pp. 473-478
    • Levy, H.R.1    Christoff, M.2    Ingulli, J.3    Ho, E.M.4
  • 22
    • 0036375584 scopus 로고    scopus 로고
    • Recombinant human glucose-6-phosphate dehydrogenase. Evidence for a rapid equilibrium random-order mechanism
    • X.-T. Wang, S.W.N. Au, V.M.S. Lam, and P.C. Engel Recombinant human glucose-6-phosphate dehydrogenase. Evidence for a rapid equilibrium random-order mechanism European Journal of Biochemistry 269 2002 3417 3424
    • (2002) European Journal of Biochemistry , vol.269 , pp. 3417-3424
    • Wang, X.-T.1    Au, S.W.N.2    Lam, V.M.S.3    Engel, P.C.4
  • 23
    • 0031776077 scopus 로고    scopus 로고
    • The role of reactive oxygen species in adriamycin and menadione-induced glomerular toxicity
    • W.A. Morgan, B. Kaler, and P.H. Bach The role of reactive oxygen species in adriamycin and menadione-induced glomerular toxicity Toxicol. Lett. 94 1998 209 215
    • (1998) Toxicol. Lett. , vol.94 , pp. 209-215
    • Morgan, W.A.1    Kaler, B.2    Bach, P.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.