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Volumn 3, Issue 1, 2007, Pages 13-17

Determination of volatile products of human colon cell line metabolism by GC/MS analysis

Author keywords

GC MS; Human colon cell lines; Metabolic pathways; Metabolomics; SPME; Volatile metabolites

Indexed keywords


EID: 33947418422     PISSN: 15733882     EISSN: 15733890     Source Type: Journal    
DOI: 10.1007/s11306-006-0038-y     Document Type: Article
Times cited : (71)

References (19)
  • 1
    • 0018381417 scopus 로고
    • Human liver pi-alcohol dehydrogenase: Kinetic and molecular properties
    • Bosron W.F., Li T.K., Dafeldecker W.P., Vallee B.L. (1979). Human liver pi-alcohol dehydrogenase: Kinetic and molecular properties. Biochemistry 6:1101-1105
    • (1979) Biochemistry , vol.6 , pp. 1101-1105
    • Bosron, W.F.1    Li, T.K.2    Dafeldecker, W.P.3    Vallee, B.L.4
  • 2
    • 0030053438 scopus 로고    scopus 로고
    • Influence of substrate structure on the catalytic efficiency of hydroxysteroid sulfotransferase STa in the sulfation of alcohols
    • Chen G., Banoglu E., Duffel M.W. (1996). Influence of substrate structure on the catalytic efficiency of hydroxysteroid sulfotransferase STa in the sulfation of alcohols. Chem. Res. Toxicol. 9:67-74
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 67-74
    • Chen, G.1    Banoglu, E.2    Duffel, M.W.3
  • 3
    • 0037067751 scopus 로고    scopus 로고
    • Kinetic mechanism of human class IV alcohol dehydrogenase functioning as retinol dehydrogenase
    • Chou C.F., Lai C.L., Chang Y., Cuester G., Yin S.J. (2002). Kinetic mechanism of human class IV alcohol dehydrogenase functioning as retinol dehydrogenase. J. Biol. Chem. 277:25209-25216
    • (2002) J. Biol. Chem. , vol.277 , pp. 25209-25216
    • Chou, C.F.1    Lai, C.L.2    Chang, Y.3    Cuester, G.4    Yin, S.J.5
  • 5
    • 0029863799 scopus 로고    scopus 로고
    • Kinetics and specifity of human liver aldehyde dehydrogenases toward aliphatic, aromatic, and fused polycyclic aldehydes
    • Klyosov A.A. (1996). Kinetics and specifity of human liver aldehyde dehydrogenases toward aliphatic, aromatic, and fused polycyclic aldehydes. Biochemistry 35:4457-4467
    • (1996) Biochemistry , vol.35 , pp. 4457-4467
    • Klyosov, A.A.1
  • 6
    • 0036182468 scopus 로고    scopus 로고
    • Characterization of the Saccharomyces cervisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: Relevance in aldehyde reduction
    • Larroy C., Fernandesz M.R., Gonzalez E., Pares X., Biosca J.A. (2002). Characterization of the Saccharomyces cervisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction. Biochem. J. 361:163-172
    • (2002) Biochem. J. , vol.361 , pp. 163-172
    • Larroy, C.1    Fernandesz, M.R.2    Gonzalez, E.3    Pares, X.4    Biosca, J.A.5
  • 7
    • 0018366069 scopus 로고
    • Characterization of fatty alcohol: NAD + oxidoreductase from rat liver
    • Lee T. (1979). Characterization of fatty alcohol: NAD + oxidoreductase from rat liver. J. Biol. Chem. 254:2892-2896
    • (1979) J. Biol. Chem. , vol.254 , pp. 2892-2896
    • Lee, T.1
  • 10
    • 0043069547 scopus 로고    scopus 로고
    • Understanding global systems biology: Metabonomics and the continuum of metabolism
    • Nicholson J.K., Wilson I.D. (2003). Understanding global systems biology: Metabonomics and the continuum of metabolism. Nat. Rev. Drug Discov. 8:668-676
    • (2003) Nat. Rev. Drug Discov. , vol.8 , pp. 668-676
    • Nicholson, J.K.1    Wilson, I.D.2
  • 12
    • 0034218717 scopus 로고    scopus 로고
    • Simultaneous analysis of metabolites in potato tuber by gas chromatography-mass spectrometry
    • Roessner U., Wagner C., Kopka J., Trethewey R.N., Willmitzer L.(2000). Simultaneous analysis of metabolites in potato tuber by gas chromatography-mass spectrometry. Plant J. 23:31-142
    • (2000) Plant J. , vol.23 , pp. 31-142
    • Roessner, U.1    Wagner, C.2    Kopka, J.3    Trethewey, R.N.4    Willmitzer, L.5
  • 13
    • 0001595128 scopus 로고
    • Purification and properties of secondary alcohol oxidase with an acidic isoelectric point
    • Sakai K., Hamada N., Watanabe Y. (1985). Purification and properties of secondary alcohol oxidase with an acidic isoelectric point. Agric. Biol. Chem. 49:817-825
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 817-825
    • Sakai, K.1    Hamada, N.2    Watanabe, Y.3
  • 15
    • 0005958575 scopus 로고    scopus 로고
    • Enzyme data and metabolic information: BRENDA, a resource for research biology, biochemistry and medicine
    • Schomburg I., Hofmann O., Bänsch C., Chang A., Schomburg D. (2000). Enzyme data and metabolic information: BRENDA, a resource for research biology, biochemistry and medicine. Gene Funct. Dis. 3, 4:109-118
    • (2000) Gene Funct. Dis. , vol.3-4 , pp. 109-118
    • Schomburg, I.1    Hofmann, O.2    Bänsch, C.3    Chang, A.4    Schomburg, D.5
  • 17
    • 0030300931 scopus 로고    scopus 로고
    • Combined HPLC, NMR spectroscopy, and ion-trap mass spectrometry with application to the detection and characterization of xenobiotic and endogenous metabolites in human urine
    • Shockcor J.P., Unger S.E., Wilson I.D., Foxall P.J.D., Nicholson J.K., Lindon J.C. (1996). Combined HPLC, NMR spectroscopy, and ion-trap mass spectrometry with application to the detection and characterization of xenobiotic and endogenous metabolites in human urine. Anal. Chem. 68:4431-4435
    • (1996) Anal. Chem. , vol.68 , pp. 4431-4435
    • Shockcor, J.P.1    Unger, S.E.2    Wilson, I.D.3    Foxall, P.J.D.4    Nicholson, J.K.5    Lindon, J.C.6
  • 19
    • 0017406572 scopus 로고
    • Purification and properties of NADPH-dependent aldehyde reductase from human liver
    • Wermuth B., Munch J.D., von Wartburg J.P. (1977). Purification and properties of NADPH-dependent aldehyde reductase from human liver. J. Biol. Chem. 252(11):3821-3828
    • (1977) J. Biol. Chem. , vol.252 , Issue.11 , pp. 3821-3828
    • Wermuth, B.1    Munch, J.D.2    von Wartburg, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.