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Volumn 42, Issue 2, 2003, Pages 87-99

Characterisation of G418-induced metabolic load in recombinant CHO and BHK cells: Effect on the activity and expression of central metabolic enzymes

Author keywords

BHK; CHO; Enzymes; G418; Metabolic load; Metabolism; RT PCR

Indexed keywords

ANTIBIOTIC G 418; CELL ENZYME; CELL EXTRACT; CELL PROTEIN; GASTRIC INHIBITORY POLYPEPTIDE; GASTRIC INHIBITORY POLYPEPTIDE RECEPTOR; GLUCAGON RECEPTOR; GLUCOSE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTAMATE AMMONIA LIGASE; GLUTAMATE DEHYDROGENASE; GLUTAMINASE; GLUTAMINE; LACTATE DEHYDROGENASE; LACTIC ACID; MEMBRANE RECEPTOR; PYRUVATE CARBOXYLASE; RECOMBINANT RECEPTOR; UNCLASSIFIED DRUG;

EID: 1642460583     PISSN: 09209069     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:CYTO.0000009821.82741.8c     Document Type: Article
Times cited : (17)

References (66)
  • 2
    • 0017279627 scopus 로고
    • Activities of citrate synthase and NAD-linked and NADP-linked isocitrate dehydrogenase in muscle from vertebrates and invertebrates
    • Alp P.R., Newsholme E.A. and Zammit V.A. 1976. Activities of citrate synthase and NAD-linked and NADP-linked isocitrate dehydrogenase in muscle from vertebrates and invertebrates. Biochem. J. 154: 689-700.
    • (1976) Biochem. J. , vol.154 , pp. 689-700
    • Alp, P.R.1    Newsholme, E.A.2    Zammit, V.A.3
  • 3
    • 0035971196 scopus 로고    scopus 로고
    • Regulation of the processing of glucose-6-phosphate dehydrogenase mRNA by nutritional status
    • Amir-Ahmady B. and Salati L.M. 2001. Regulation of the processing of glucose-6-phosphate dehydrogenase mRNA by nutritional status. J. Biol. Chem. 276: 10514-10523.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10514-10523
    • Amir-Ahmady, B.1    Salati, L.M.2
  • 4
    • 0020617998 scopus 로고
    • Glutamine metabolism in lymphocytes of the rat
    • Ardawi M.S.M. and Newsholme E.A. 1983. Glutamine metabolism in lymphocytes of the rat. Biochem. J. 212: 835-842.
    • (1983) Biochem. J. , vol.212 , pp. 835-842
    • Ardawi, M.S.M.1    Newsholme, E.A.2
  • 5
    • 0014013130 scopus 로고
    • Apparent cooperative effect of acetyl-CoA on sheep kidney pyruvate carboxylase
    • Barrit G.J., Keech D.B. and Ling A.M. 1966. Apparent cooperative effect of acetyl-CoA on sheep kidney pyruvate carboxylase. Biochem. Biophys. Res. Commun. 24: 476-481.
    • (1966) Biochem. Biophys. Res. Commun. , vol.24 , pp. 476-481
    • Barrit, G.J.1    Keech, D.B.2    Ling, A.M.3
  • 6
    • 0025405549 scopus 로고
    • Plasmid-encoded protein: The principal factor in the 'metabolic burden' associated with recombinant bacteria
    • Bentley W.E., Mirjalili N., Andersen D.C., Davis R.H. and Kompala D.S. 1990. Plasmid-encoded protein: The principal factor in the 'metabolic burden' associated with recombinant bacteria. Biotechnol. Bioeng. 35: 668-681.
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 668-681
    • Bentley, W.E.1    Mirjalili, N.2    Andersen, D.C.3    Davis, R.H.4    Kompala, D.S.5
  • 7
    • 0024672816 scopus 로고
    • Effects of plasmid amplification and recombinant gene expression on the growth kinetics of recombinant Escherichia coli
    • Betenbaugh M.J., Beaty C. and Dhurjati P. 1989. Effects of plasmid amplification and recombinant gene expression on the growth kinetics of recombinant Escherichia coli. Biotechnol. Bioeng. 33: 1425-1436.
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 1425-1436
    • Betenbaugh, M.J.1    Beaty, C.2    Dhurjati, P.3
  • 9
    • 0021824122 scopus 로고
    • Glutamine and glucose metabolism during thymocyte proliferation: Pathways of glutamine and glutamate metabolism
    • Brand K. 1985. Glutamine and glucose metabolism during thymocyte proliferation: Pathways of glutamine and glutamate metabolism. Biochem. J. 228: 353-361.
    • (1985) Biochem. J. , vol.228 , pp. 353-361
    • Brand, K.1
  • 10
    • 0033527072 scopus 로고    scopus 로고
    • The adaptation of BHK cells to a non-ammoniagenic glutamate-based culture medium
    • Christie A. and Butler M. 1999. The adaptation of BHK cells to a non-ammoniagenic glutamate-based culture medium. Biotechnol. Bioeng. 64: 298-309.
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 298-309
    • Christie, A.1    Butler, M.2
  • 11
    • 0031862830 scopus 로고    scopus 로고
    • Determinants of glutamine dependence and utilisation by normal and tumor-derived breast cell lines
    • Collins C.L., Wasa M., Souba W.W. and Abcouwer S.F. 1998. Determinants of glutamine dependence and utilisation by normal and tumor-derived breast cell lines. J. Cell Physiol. 176: 166-178.
    • (1998) J. Cell Physiol. , vol.176 , pp. 166-178
    • Collins, C.L.1    Wasa, M.2    Souba, W.W.3    Abcouwer, S.F.4
  • 12
    • 0028242341 scopus 로고
    • Inhibitors of transcription such as 5,6-dichloro-1-β -D-ribofuranosylbenzimidazole and isoquinoline sulphonamide derivatives (H8 and H7) promote dephosphorylation of the carboxyl terminal domain of RNA polymerase II largest sub-unit
    • Dubois M.F., Nguyen V.T., Bellier S. and Bensuade O. 1994. Inhibitors of transcription such as 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole and isoquinoline sulphonamide derivatives (H8 and H7) promote dephosphorylation of the carboxyl terminal domain of RNA polymerase II largest sub-unit. J. Biol. Chem. 269: 13331-13336.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13331-13336
    • Dubois, M.F.1    Nguyen, V.T.2    Bellier, S.3    Bensuade, O.4
  • 13
    • 0021111993 scopus 로고
    • Regulation of the synthesis and degradation of pyruvate carboxylase in 3T3-L1 cells
    • Freytag S.O. and Utter M.F. 1983. Regulation of the synthesis and degradation of pyruvate carboxylase in 3T3-L1 cells. J. Biol. Chem. 258: 6307-6312.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6307-6312
    • Freytag, S.O.1    Utter, M.F.2
  • 14
    • 0023763120 scopus 로고
    • Catabolic control of mammalian cell culture
    • Glacken M.W. 1988. Catabolic control of mammalian cell culture. Bio/Technology 6: 1041-1050.
    • (1988) Bio/Technology , vol.6 , pp. 1041-1050
    • Glacken, M.W.1
  • 15
    • 0027022939 scopus 로고
    • Effect of amplification of dhfr and lacZ genes on growth and β-galactosidase expression in suspension cultures of recombinant CHO cells
    • Gu M.B., Kern J.A., Todd P. and Kompala D.S. 1992. Effect of amplification of dhfr and lacZ genes on growth and β-galactosidase expression in suspension cultures of recombinant CHO cells. Cytotechnology 9: 237-245.
    • (1992) Cytotechnology , vol.9 , pp. 237-245
    • Gu, M.B.1    Kern, J.A.2    Todd, P.3    Kompala, D.S.4
  • 16
    • 0030066488 scopus 로고    scopus 로고
    • Metabolic burden in recombinant CHO cells: Effect of dhfr gene amplification and lacZ expression
    • Gu M.B., Todd P. and Kompala D.S. 1996. Metabolic burden in recombinant CHO cells: effect of dhfr gene amplification and lacZ expression. Cytotechnology 18: 159-166.
    • (1996) Cytotechnology , vol.18 , pp. 159-166
    • Gu, M.B.1    Todd, P.2    Kompala, D.S.3
  • 17
    • 0002548987 scopus 로고
    • Energetics of glutaminolysis - A theoretical evaluation
    • Spier R.E., Griffiths J.B. and Meignier B. (eds). Butterworth-Heinemann Ltd., Oxford
    • Haggstrom L. 1991. Energetics of glutaminolysis - a theoretical evaluation. In: Spier R.E., Griffiths J.B. and Meignier B. (eds), Production of Biologicals from Animal Cells in Culture. Butterworth-Heinemann Ltd., Oxford, pp. 79-81.
    • (1991) Production of Biologicals from Animal Cells in Culture , pp. 79-81
    • Haggstrom, L.1
  • 18
    • 0029779966 scopus 로고    scopus 로고
    • The 3′-non-translated region of rat renal glutaminase mRNA contains a pH-responsive stability element
    • Hansen W.R., Barsic-Tress N., Taylor L. and Curthoys N.P. 1996. The 3′-non-translated region of rat renal glutaminase mRNA contains a pH-responsive stability element. Am. J. Physiol. 271: F126-F131.
    • (1996) Am. J. Physiol. , vol.271
    • Hansen, W.R.1    Barsic-Tress, N.2    Taylor, L.3    Curthoys, N.P.4
  • 19
    • 0025742913 scopus 로고
    • Effect of acute alterations in acid-base balance on rat renal glutaminase and phosphoenol-pyruvate carboxykinase gene expression
    • Hwang J.-J. and Curthoys N.P. 1991. Effect of acute alterations in acid-base balance on rat renal glutaminase and phosphoenol-pyruvate carboxykinase gene expression. J. Biol. Chem. 266: 9392-9396.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9392-9396
    • Hwang, J.-J.1    Curthoys, N.P.2
  • 20
    • 0025718642 scopus 로고
    • Mechanism of altered renal glutaminase gene expression in response to chronic acidosis
    • Hwang J.-J., Perera S., Shapiro R.A. and Curthoys N.P. 1991. Mechanism of altered renal glutaminase gene expression in response to chronic acidosis. Biochemistry 30: 7522-7526.
    • (1991) Biochemistry , vol.30 , pp. 7522-7526
    • Hwang, J.-J.1    Perera, S.2    Shapiro, R.A.3    Curthoys, N.P.4
  • 21
    • 0033385223 scopus 로고    scopus 로고
    • Improvement of the primary metabolism of cell cultures by introducing a new cytoplasmic pyruvate carboxylase reaction
    • Irani N., Wirth M., van den Heuvel J. and Wagner R. 1999. Improvement of the primary metabolism of cell cultures by introducing a new cytoplasmic pyruvate carboxylase reaction. Biotechnol. Bioeng. 86: 238-246.
    • (1999) Biotechnol. Bioeng. , vol.86 , pp. 238-246
    • Irani, N.1    Wirth, M.2    Van Den Heuvel, J.3    Wagner, R.4
  • 22
    • 0026560877 scopus 로고
    • Characterisation of glutamine metabolism in two related murine hybridomas
    • Jenkins H.A., Butler M. and Dickson A.J. 1992. Characterisation of glutamine metabolism in two related murine hybridomas. J. Biotechnol. 23: 167-182.
    • (1992) J. Biotechnol. , vol.23 , pp. 167-182
    • Jenkins, H.A.1    Butler, M.2    Dickson, A.J.3
  • 23
    • 0030601137 scopus 로고    scopus 로고
    • Identification of novel alternatively spliced pyruvate carboxylase mRNAs with divergent 5′-untranslated regions, which are epressed in a tissue-specific manner
    • Jitrapakdee S., Walker M.E. and Wallace J.C. 1996. Identification of novel alternatively spliced pyruvate carboxylase mRNAs with divergent 5′-untranslated regions, which are epressed in a tissue-specific manner. Biochem. Biophys. Res. Comm. 223: 695-700.
    • (1996) Biochem. Biophys. Res. Comm. , vol.223 , pp. 695-700
    • Jitrapakdee, S.1    Walker, M.E.2    Wallace, J.C.3
  • 24
    • 0030795098 scopus 로고    scopus 로고
    • The rat pyruvate carboxylase gene structure: Alternate promoters generate multiple transcripts with 5′-end heterogeneity
    • Jitrapakdee S., Booker G.W., Cassady A.I. and Wallace J.C. 1997. The rat pyruvate carboxylase gene structure: Alternate promoters generate multiple transcripts with 5′-end heterogeneity. J. Biol. Chem. 272: 20522-20530.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20522-20530
    • Jitrapakdee, S.1    Booker, G.W.2    Cassady, A.I.3    Wallace, J.C.4
  • 25
    • 0032545425 scopus 로고    scopus 로고
    • Regulation of rat pyruvate carboxylase gene expression by alternate promoters during development in genetically obese rats and in insulin secreting cells
    • Jitrapakdee S., Gong Q., MacDonald M.J. and Wallace J.C. 1998. Regulation of rat pyruvate carboxylase gene expression by alternate promoters during development in genetically obese rats and in insulin secreting cells. J. Biol. Chem. 273: 34422-34428.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34422-34428
    • Jitrapakdee, S.1    Gong, Q.2    MacDonald, M.J.3    Wallace, J.C.4
  • 27
    • 0030704158 scopus 로고    scopus 로고
    • Comparison of heat flux in wild type and genetically engineered chinese hamster ovary cells
    • Kidane A.H., Guan Y., Evans P.M., Kaderbhai M.A. and Kemp R.B. 1997. Comparison of heat flux in wild type and genetically engineered chinese hamster ovary cells. J. Thermal Analysis 49: 771-783.
    • (1997) J. Thermal Analysis , vol.49 , pp. 771-783
    • Kidane, A.H.1    Guan, Y.2    Evans, P.M.3    Kaderbhai, M.A.4    Kemp, R.B.5
  • 28
    • 0028835484 scopus 로고
    • Oxidation of glucose carbon entering the TCA cycle is reduced by glutamine in small intestine epithelial cells
    • Kight C.E. and Fleming S.E. 1995. Oxidation of glucose carbon entering the TCA cycle is reduced by glutamine in small intestine epithelial cells. Am. J. Physiol. 268: G879-G888.
    • (1995) Am. J. Physiol. , vol.268
    • Kight, C.E.1    Fleming, S.E.2
  • 29
    • 0002598959 scopus 로고    scopus 로고
    • Characterisation of chimeric antibody-producing CHO cells in the course of dihydrofolate reductase-mediated gene amplification and their stability in the absence of selective pressure
    • Kim S.J., Kim N.S., Ryu C.J., Hong H.J. and Lee G.M. 1998. Characterisation of chimeric antibody-producing CHO cells in the course of dihydrofolate reductase-mediated gene amplification and their stability in the absence of selective pressure. Biotechnol. Bioeng. 58: 73-84.
    • (1998) Biotechnol. Bioeng. , vol.58 , pp. 73-84
    • Kim, S.J.1    Kim, N.S.2    Ryu, C.J.3    Hong, H.J.4    Lee, G.M.5
  • 30
    • 0035937134 scopus 로고    scopus 로고
    • Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal regulating kinase 1
    • Ko Y.-G., Kim E.-K., Kim T., Park H., Park H.-S., Choi E.-J. and Kim S. 2001. Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal regulating kinase 1. J. Biol. Chem. 276: 6030-6036.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6030-6036
    • Ko, Y.-G.1    Kim, E.-K.2    Kim, T.3    Park, H.4    Park, H.-S.5    Choi, E.-J.6    Kim, S.7
  • 31
    • 0032191161 scopus 로고    scopus 로고
    • Quantitation of glutaminase mRNA in enterocytes using competitive RT-PCR
    • Kong S.-E., Heel K.A., Hall J.C. and McCauley R.D. 1998. Quantitation of glutaminase mRNA in enterocytes using competitive RT-PCR. Mol. Cell Probes 12: 339-341.
    • (1998) Mol. Cell Probes , vol.12 , pp. 339-341
    • Kong, S.-E.1    Heel, K.A.2    Hall, J.C.3    McCauley, R.D.4
  • 32
    • 0015848629 scopus 로고
    • Regulation of glutamine synthetase activity of hepatoma tissue culture cells by glutamine and dexamethasone
    • Kulka R.G. and Cohen H. 1973. Regulation of glutamine synthetase activity of hepatoma tissue culture cells by glutamine and dexamethasone. J. Biol. Chem. 248: 6738-6743.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6738-6743
    • Kulka, R.G.1    Cohen, H.2
  • 35
    • 0030923984 scopus 로고    scopus 로고
    • Identification of an mRNA-binding protein and the specific elements that may mediate the pH-responsive induction of renal glutaminase mRNA
    • Laterza O.F., Hansen W.R., Taylor L. and Curthoys N.P. 1997. Identification of an mRNA-binding protein and the specific elements that may mediate the pH-responsive induction of renal glutaminase mRNA. J. Biol. Chem. 272: 22481-22488.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22481-22488
    • Laterza, O.F.1    Hansen, W.R.2    Taylor, L.3    Curthoys, N.P.4
  • 36
    • 0033843976 scopus 로고    scopus 로고
    • Effect of acidosis on the properties of the glutaminase mRNA pH-response element binding protein
    • Laterza O.F. and Curthoys N.P. 2000. Effect of acidosis on the properties of the glutaminase mRNA pH-response element binding protein. J. Am. Soc. Nephrol. 11: 1583-1588.
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 1583-1588
    • Laterza, O.F.1    Curthoys, N.P.2
  • 37
    • 0031194880 scopus 로고    scopus 로고
    • Stochiometry, kinetics and regulation of glucose and amino acid metabolism of a recombinant BHK cell line in batch and continuous culture
    • Linz M., Zeng A.-P., Wagner R. and Deckwer W.-D. 1997. Stochiometry, kinetics and regulation of glucose and amino acid metabolism of a recombinant BHK cell line in batch and continuous culture. Biotechnol. Prog. 13: 453-463.
    • (1997) Biotechnol. Prog. , vol.13 , pp. 453-463
    • Linz, M.1    Zeng, A.-P.2    Wagner, R.3    Deckwer, W.-D.4
  • 38
    • 0025864495 scopus 로고
    • The 5′ untranslated regions of acetyl coenzyme A carboxylase mRNA provide specific translational control in vivo
    • Lopez-Casillas F. and Kim K.-H. 1991. The 5′ untranslated regions of acetyl coenzyme A carboxylase mRNA provide specific translational control in vivo. Eur. J. Biochem. 201: 119-127.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 119-127
    • Lopez-Casillas, F.1    Kim, K.-H.2
  • 39
    • 0001416199 scopus 로고
    • Glutamine: Determination with glutaminase and glutamate dehydrogenase
    • Bergmeyer H.U. (ed.). Academic Press, London
    • Lund P. 1974. Glutamine: Determination with glutaminase and glutamate dehydrogenase. In: Bergmeyer H.U. (ed.), Methods of Enzymatic Analysis. Vol. 4:. Academic Press, London, pp. 1719-1722.
    • (1974) Methods of Enzymatic Analysis , vol.4 , pp. 1719-1722
    • Lund, P.1
  • 41
    • 0015217922 scopus 로고
    • Rat liver pyruvate carboxylase IV: Factors that affect the regulation in vivo
    • McClure W.R. and Lardy H.A. 1971. Rat liver pyruvate carboxylase IV: factors that affect the regulation in vivo. J. Biol. Chem. 246: 3591-3596.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3591-3596
    • McClure, W.R.1    Lardy, H.A.2
  • 42
    • 0030049769 scopus 로고    scopus 로고
    • Comparative analysis of glucose and glutamine metabolism in transformed mammalian cell lines, insect and primary liver cells
    • Neerman J. and Wagner R. 1996. Comparative analysis of glucose and glutamine metabolism in transformed mammalian cell lines, insect and primary liver cells. J. Cell Physiol. 166: 152-169.
    • (1996) J. Cell Physiol. , vol.166 , pp. 152-169
    • Neerman, J.1    Wagner, R.2
  • 43
    • 0021792065 scopus 로고
    • The role of high rates of glycolysis and glutamine utilisation in rapidly dividing cells
    • Newsholme E.A., Crabtree B. and Ardawi M.S.M. 1985. The role of high rates of glycolysis and glutamine utilisation in rapidly dividing cells. Biosci. Rep. 5: 393-400.
    • (1985) Biosci. Rep. , vol.5 , pp. 393-400
    • Newsholme, E.A.1    Crabtree, B.2    Ardawi, M.S.M.3
  • 44
    • 0014599987 scopus 로고
    • Pyruvate Carboxylase in Rhodopseudomonas spheroides
    • Payne J. and Morris J.G. 1969. Pyruvate Carboxylase in Rhodopseudomonas spheroides. J. Gen. Microbiol. 59: 97-101.
    • (1969) J. Gen. Microbiol. , vol.59 , pp. 97-101
    • Payne, J.1    Morris, J.G.2
  • 45
    • 0027112480 scopus 로고
    • Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells
    • Pendse G.J., Karkare S. and Bailey J.E. 1992. Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells. Biotechnol. Bioeng. 40: 119-129.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 119-129
    • Pendse, G.J.1    Karkare, S.2    Bailey, J.E.3
  • 46
    • 0024670307 scopus 로고
    • Kinetics of growth and glucose transport in glucose limited chemostat cultures of Saccharomyces cerevisiae CBS 8066
    • Postma E., Scheffers W.A. and van Dijken J.P. 1989. Kinetics of growth and glucose transport in glucose limited chemostat cultures of Saccharomyces cerevisiae CBS 8066. Yeast 5: 159-165.
    • (1989) Yeast , vol.5 , pp. 159-165
    • Postma, E.1    Scheffers, W.A.2    Van Dijken, J.P.3
  • 47
    • 0024615221 scopus 로고
    • Enzymic analysis of the Crabtree effect in glucose-limiting chemostat cultures of Saccharomyces cerevisiae
    • Postma E., Verduyn C., Scheffers W.A. and van Dijken J.P. 1989. Enzymic analysis of the Crabtree effect in glucose-limiting chemostat cultures of Saccharomyces cerevisiae. Appl. Environ. Microbiol. 55: 468-477.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 468-477
    • Postma, E.1    Verduyn, C.2    Scheffers, W.A.3    Van Dijken, J.P.4
  • 48
    • 0030439179 scopus 로고    scopus 로고
    • Effects of starvation, diabetes and carbon tetrachloride intoxication on rat kidney cortex and liver pyruvate carboxylase levels
    • Salto R., Sola M., Oliver F.J. and Vargas A.M. 1996. Effects of starvation, diabetes and carbon tetrachloride intoxication on rat kidney cortex and liver pyruvate carboxylase levels. Arch. Physiol. Biochem. 104: 845-850.
    • (1996) Arch. Physiol. Biochem. , vol.104 , pp. 845-850
    • Salto, R.1    Sola, M.2    Oliver, F.J.3    Vargas, A.M.4
  • 49
    • 0032833833 scopus 로고    scopus 로고
    • Evolution of pyruvate carboxylase and other biotin containing enzymes in developing rat liver and kidney
    • Salto R., Giron M.D., Sola M. and Vargas M. 1999. Evolution of pyruvate carboxylase and other biotin containing enzymes in developing rat liver and kidney. Mol. Cell Biochem. 200: 111-117.
    • (1999) Mol. Cell Biochem. , vol.200 , pp. 111-117
    • Salto, R.1    Giron, M.D.2    Sola, M.3    Vargas, M.4
  • 50
    • 0033613855 scopus 로고    scopus 로고
    • Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression
    • Salvemini F., Franze A., Iervolino A., Filosa S., Salzano S. and Ursini M.V. 1999. Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression. J. Biol. Chem. 274: 2750-2757.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2750-2757
    • Salvemini, F.1    Franze, A.2    Iervolino, A.3    Filosa, S.4    Salzano, S.5    Ursini, M.V.6
  • 51
    • 0033526894 scopus 로고    scopus 로고
    • Effect of glutamine limitiation on the death of attached Chinese Hamster Ovary cells
    • Sanfeliu A. and Stephanopoulous G. 1999. Effect of glutamine limitiation on the death of attached Chinese Hamster Ovary cells. Biotechnol. Bioeng. 64: 46-53.
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 46-53
    • Sanfeliu, A.1    Stephanopoulous, G.2
  • 52
    • 0003175895 scopus 로고
    • Glutamate dehydrogenase
    • Bergmeyer H.U. (ed.). Academic Press, New York
    • Schmidt E. and Schmidt F.W. 1983. Glutamate dehydrogenase. In: Bergmeyer H.U. (ed.), Methods of Enzymatic Analysis. Vol. 3:. Academic Press, New York, pp. 216-227.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 216-227
    • Schmidt, E.1    Schmidt, F.W.2
  • 53
    • 0345960852 scopus 로고    scopus 로고
    • Overexpression of recombinant human antithrombin III in Chinese hamster ovary cells results in malformation and decreased secretion of recombinant protein
    • Schroder M. and Friedl P. 1997. Overexpression of recombinant human antithrombin III in Chinese hamster ovary cells results in malformation and decreased secretion of recombinant protein. Biotechnol. Bioeng. 53: 547-559.
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 547-559
    • Schroder, M.1    Friedl, P.2
  • 54
    • 0022407889 scopus 로고
    • Effects of recombinant plasmid content on growth properties and cloned gene product formation in Escherichia coli
    • Seo J.-H. and Bailey J.E. 1985. Effects of recombinant plasmid content on growth properties and cloned gene product formation in Escherichia coli. Biotechnol. Bioeng. 27: 1668-1674.
    • (1985) Biotechnol. Bioeng. , vol.27 , pp. 1668-1674
    • Seo, J.-H.1    Bailey, J.E.2
  • 55
    • 0023852943 scopus 로고
    • Epidermal growth factor rapidly activates the hexose monophosphate shunt in kidney cells
    • Stanton R.C. and Seifter J.L. 1988. Epidermal growth factor rapidly activates the hexose monophosphate shunt in kidney cells. Am. J. Physiol. 254: C267-C271.
    • (1988) Am. J. Physiol. , vol.254
    • Stanton, R.C.1    Seifter, J.L.2
  • 56
    • 0025851376 scopus 로고
    • Rapid release of bound glucose-6-phosphate dehydrogenase by growth factors
    • Stanton R.C., Seifter J.L., Boxer D.C., Zimmerman E. and Cantley L.C. 1991. Rapid release of bound glucose-6-phosphate dehydrogenase by growth factors. J. Biol. Chem. 266: 12442-12448.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12442-12448
    • Stanton, R.C.1    Seifter, J.L.2    Boxer, D.C.3    Zimmerman, E.4    Cantley, L.C.5
  • 59
    • 0016615112 scopus 로고
    • Activities of citrate synthase, NAD-linked and NADP-linked isocitrate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase and alanine aminotransferase in nervous tissue from vertebrates and invertebrates
    • Sugden P.M. and Newsholme E.A. 1975. Activities of citrate synthase, NAD-linked and NADP-linked isocitrate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase and alanine aminotransferase in nervous tissue from vertebrates and invertebrates. Biochem. J. 150: 105-111.
    • (1975) Biochem. J. , vol.150 , pp. 105-111
    • Sugden, P.M.1    Newsholme, E.A.2
  • 60
    • 0003139427 scopus 로고
    • Prusiner S. and Stadtman E.R. (eds). Academic Press, New York
    • Tate S.S. and Meister A. 1973. In: Prusiner S. and Stadtman E.R. (eds), The Enzymes of Glutamine Metabolism. Academic Press, New York, pp. 77-125.
    • (1973) The Enzymes of Glutamine Metabolism , pp. 77-125
    • Tate, S.S.1    Meister, A.2
  • 61
    • 0028229095 scopus 로고
    • Signal transduction proteins that associate with the platelet-derived growth factor (PDGF) receptor mediate the PDGF-induced release of glucose-6-phosphate dehydrogenase from permeabilised cells
    • Tian W.-N., Pignatare J.N. and Stanton R.C. 1994. Signal transduction proteins that associate with the platelet-derived growth factor (PDGF) receptor mediate the PDGF-induced release of glucose-6-phosphate dehydrogenase from permeabilised cells. J. Biol. Chem. 269: 14798-14805.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14798-14805
    • Tian, W.-N.1    Pignatare, J.N.2    Stanton, R.C.3
  • 63
    • 0000191753 scopus 로고
    • Lactate dehydrogenase, UV method with pyruvate and NADH
    • Bergmeyer H.U. (ed.). Academic Press, New York
    • Vassault A. 1983. Lactate dehydrogenase, UV method with pyruvate and NADH. In: Bergmeyer H.U. (ed.), Methods of Enzymatic Analysis. Vol. 3:. Academic Press, New York, pp. 118-126.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 118-126
    • Vassault, A.1
  • 64
    • 0032486571 scopus 로고    scopus 로고
    • Fluxes and enzyme activities in central metabolism of myeloma cells grown in chemostat culture
    • Vriezen N. and van Dijken J.P. 1998. Fluxes and enzyme activities in central metabolism of myeloma cells grown in chemostat culture. Biotechnol. Bioeng. 59: 28-39.
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 28-39
    • Vriezen, N.1    Van Dijken, J.P.2
  • 65
    • 0034789843 scopus 로고    scopus 로고
    • The effects of G418 on the growth and metabolism of recombinant mammalian cell lines
    • Yallop, C.A. and Svendsen I. 2001. The effects of G418 on the growth and metabolism of recombinant mammalian cell lines. Cytotechnology 35: 101-114.
    • (2001) Cytotechnology , vol.35 , pp. 101-114
    • Yallop, C.A.1    Svendsen, I.2
  • 66
    • 0028842233 scopus 로고
    • Regulation of pyruvate carboxylase in 3T3-L1 cells
    • Zhang J., Xia W.-L. and Ahmad F. 1995. Regulation of pyruvate carboxylase in 3T3-L1 cells. Biochem. J. 306: 205-210.
    • (1995) Biochem. J. , vol.306 , pp. 205-210
    • Zhang, J.1    Xia, W.-L.2    Ahmad, F.3


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