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Volumn 261, Issue 2, 2009, Pages 318-329

Simultaneous interaction of enzymes with two modifiers: Reappraisal of kinetic models and new paradigms

Author keywords

Activation; Antagonism; Double inhibition; Enzyme kinetics; Synergy

Indexed keywords

ANTAGONISM; BIOLOGY; ENZYME ACTIVITY; INHIBITOR; MODELING; REACTION KINETICS; SYNERGISM; THEORETICAL STUDY;

EID: 70349776038     PISSN: 00225193     EISSN: 10958541     Source Type: Journal    
DOI: 10.1016/j.jtbi.2009.07.033     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 0024415184 scopus 로고
    • Inhibition kinetics of acetylcholinesterase with fluoromethyl ketones
    • Allen K.N., and Abeles R.H. Inhibition kinetics of acetylcholinesterase with fluoromethyl ketones. Biochemistry 28 (1989) 8466-8473
    • (1989) Biochemistry , vol.28 , pp. 8466-8473
    • Allen, K.N.1    Abeles, R.H.2
  • 2
    • 0029800892 scopus 로고    scopus 로고
    • Analysis of the interactions between an enzyme and multiple inhibitors using combination plots
    • Asante-Appiah E., and Chan W.W. Analysis of the interactions between an enzyme and multiple inhibitors using combination plots. Biochem. J. 320 Pt 1 (1996) 17-26
    • (1996) Biochem. J. , vol.320 , Issue.PART 1 , pp. 17-26
    • Asante-Appiah, E.1    Chan, W.W.2
  • 3
    • 0029865072 scopus 로고    scopus 로고
    • Synergistic binding of inhibitors to the protease from HIV type 1
    • Asante-Appiah E., and Chan W.W. Synergistic binding of inhibitors to the protease from HIV type 1. Biochem. J. 315 Pt 1 (1996) 113-137
    • (1996) Biochem. J. , vol.315 , Issue.PART 1 , pp. 113-137
    • Asante-Appiah, E.1    Chan, W.W.2
  • 4
    • 0019617042 scopus 로고
    • The specific velocity plot. A graphical method for determining inhibition parameters for both linear and hyperbolic enzyme inhibitors
    • 10.1111/j.1432-1033.1981.tb05570.x
    • Baici A. The specific velocity plot. A graphical method for determining inhibition parameters for both linear and hyperbolic enzyme inhibitors. Eur. J. Biochem. 119 (1981) 9-14 10.1111/j.1432-1033.1981.tb05570.x
    • (1981) Eur. J. Biochem. , vol.119 , pp. 9-14
    • Baici, A.1
  • 5
    • 0031690566 scopus 로고    scopus 로고
    • Inhibition of extracellular matrix-degrading endopeptidases: problems, comments, and hypotheses
    • Baici A. Inhibition of extracellular matrix-degrading endopeptidases: problems, comments, and hypotheses. Biol. Chem. 379 (1998) 1007-1018
    • (1998) Biol. Chem. , vol.379 , pp. 1007-1018
    • Baici, A.1
  • 6
    • 0027493879 scopus 로고
    • Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin
    • 10.1016/0006-2952(93)90321-M
    • Baici A., Diczházi C., Neszmélyi A., Móczár E., and Hornebeck W. Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin. Biochem. Pharmacol. 46 (1993) 1545-1549 10.1016/0006-2952(93)90321-M
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1545-1549
    • Baici, A.1    Diczházi, C.2    Neszmélyi, A.3    Móczár, E.4    Hornebeck, W.5
  • 7
    • 0017360661 scopus 로고
    • Synergy, additivism and antagonism in immunosuppression. A critical review
    • Berenbaum M.C. Synergy, additivism and antagonism in immunosuppression. A critical review. Clin. Exp. Immunol. 28 (1977) 1-18
    • (1977) Clin. Exp. Immunol. , vol.28 , pp. 1-18
    • Berenbaum, M.C.1
  • 9
    • 15244345391 scopus 로고    scopus 로고
    • Chiral cyclopalladated complexes derived from N,N-dimethyl-1-phenethylamine with bridging bis(diphenylphosphine)ferrocene ligand as inhibitors of the cathepsin B activity and as antitumoral agents
    • 10.1016/j.bmc.2005.01.057
    • Bincoletto C., Tersariol I.L.S., Oliveira C.R., Dreher S., Fausto D.M., Soufen M.A., Nascimento F.D., and Caires A.C.F. Chiral cyclopalladated complexes derived from N,N-dimethyl-1-phenethylamine with bridging bis(diphenylphosphine)ferrocene ligand as inhibitors of the cathepsin B activity and as antitumoral agents. Bioorg. Med. Chem. 13 (2005) 3047-3055 10.1016/j.bmc.2005.01.057
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 3047-3055
    • Bincoletto, C.1    Tersariol, I.L.S.2    Oliveira, C.R.3    Dreher, S.4    Fausto, D.M.5    Soufen, M.A.6    Nascimento, F.D.7    Caires, A.C.F.8
  • 10
    • 37049153631 scopus 로고
    • Analytical description of the effects of modifiers and of enzyme multivalency upon the steady state catalyzed reaction rate
    • Botts J., and Morales M. Analytical description of the effects of modifiers and of enzyme multivalency upon the steady state catalyzed reaction rate. Trans. Faraday Soc. 49 (1953) 696-707
    • (1953) Trans. Faraday Soc. , vol.49 , pp. 696-707
    • Botts, J.1    Morales, M.2
  • 11
    • 0025605424 scopus 로고
    • Studies on the mechanism of steroid 5-a-reductase inhibition by 3-carboxy A-ring aryl steroids
    • 10.1016/0960-0760(90)90403-8
    • Brandt M., Greway A.T., Holt D.A., Metcalf B.W., and Levy M.A. Studies on the mechanism of steroid 5-a-reductase inhibition by 3-carboxy A-ring aryl steroids. J. Steroid Biochem. Mol. Biol. 37 (1990) 575-579 10.1016/0960-0760(90)90403-8
    • (1990) J. Steroid Biochem. Mol. Biol. , vol.37 , pp. 575-579
    • Brandt, M.1    Greway, A.T.2    Holt, D.A.3    Metcalf, B.W.4    Levy, M.A.5
  • 12
    • 0017706693 scopus 로고
    • A simple generalized equation for the analysis of multiple inhibitions of Michaelis-Menten kinetic systems
    • Chou T.C., and Talalay P. A simple generalized equation for the analysis of multiple inhibitions of Michaelis-Menten kinetic systems. J. Biol. Chem. 252 (1977) 6438-6442
    • (1977) J. Biol. Chem. , vol.252 , pp. 6438-6442
    • Chou, T.C.1    Talalay, P.2
  • 13
    • 0019882480 scopus 로고
    • Generalized equations for the analysis of inhibitions of Michaelis-Menten and higher-order kinetic systems with two or more mutually exclusive and nonexclusive inhibitors
    • Chou T.C., and Talalay P. Generalized equations for the analysis of inhibitions of Michaelis-Menten and higher-order kinetic systems with two or more mutually exclusive and nonexclusive inhibitors. Eur. J. Biochem. 115 (1981) 207-216
    • (1981) Eur. J. Biochem. , vol.115 , pp. 207-216
    • Chou, T.C.1    Talalay, P.2
  • 14
    • 0022470755 scopus 로고
    • Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides
    • 10.1016/0014-5793(86)81424-7
    • Cornish-Bowden A. Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides. FEBS Lett. 203 (1986) 3-6 10.1016/0014-5793(86)81424-7
    • (1986) FEBS Lett. , vol.203 , pp. 3-6
    • Cornish-Bowden, A.1
  • 16
    • 0024445042 scopus 로고
    • Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site
    • Dunwiddie C., Thornberry N.A., Bull H.G., Sardana M., Friedman P.A., Jacobs J.W., and Simpson E. Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site. J. Biol. Chem. 264 (1989) 16694-16699
    • (1989) J. Biol. Chem. , vol.264 , pp. 16694-16699
    • Dunwiddie, C.1    Thornberry, N.A.2    Bull, H.G.3    Sardana, M.4    Friedman, P.A.5    Jacobs, J.W.6    Simpson, E.7
  • 17
    • 70349784200 scopus 로고
    • Methods of analysis of double inhibition experiments
    • Fajszi C. Methods of analysis of double inhibition experiments. Symp. Biol. Hung. 18 (1974) 77-103
    • (1974) Symp. Biol. Hung. , vol.18 , pp. 77-103
    • Fajszi, C.1
  • 18
    • 70349782776 scopus 로고
    • Kinetic basis of enzyme regulation. The triple-faced enzyme-inhibitor relation and the inhibition paradox
    • Fajszi C., and Keleti T. Kinetic basis of enzyme regulation. The triple-faced enzyme-inhibitor relation and the inhibition paradox. Symp. Biol. Hung. 18 (1974) 105-119
    • (1974) Symp. Biol. Hung. , vol.18 , pp. 105-119
    • Fajszi, C.1    Keleti, T.2
  • 19
    • 0014194856 scopus 로고
    • Mechanism of arginine biosynthesis in Chlamydomonas reindardti. II. Purification and properties of N-acetylglutamate 5-phosphotransferase, the allosteric enzyme of the pathway
    • 10.1016/0304-4165(67)90315-7
    • Faragó A., and Dénes G. Mechanism of arginine biosynthesis in Chlamydomonas reindardti. II. Purification and properties of N-acetylglutamate 5-phosphotransferase, the allosteric enzyme of the pathway. Biochim. Biophys. Acta 136 (1967) 6-18 10.1016/0304-4165(67)90315-7
    • (1967) Biochim. Biophys. Acta , vol.136 , pp. 6-18
    • Faragó, A.1    Dénes, G.2
  • 20
    • 0029831031 scopus 로고    scopus 로고
    • Antileukoprotease inhibits stratum corneum chymotryptic enzyme. Evidence for a regulative function in desquamation
    • Franzke C.W., Baici A., Bartels J., Christophers E., and Wiedow O. Antileukoprotease inhibits stratum corneum chymotryptic enzyme. Evidence for a regulative function in desquamation. J. Biol. Chem. 271 (1996) 21886-21890
    • (1996) J. Biol. Chem. , vol.271 , pp. 21886-21890
    • Franzke, C.W.1    Baici, A.2    Bartels, J.3    Christophers, E.4    Wiedow, O.5
  • 21
    • 0000832862 scopus 로고
    • An experimental research on the antagonism between the actions of physostigma and atropia
    • Fraser T.R. An experimental research on the antagonism between the actions of physostigma and atropia. Proc. R. Soc. Edin. 7 (1870-1871) 506-511
    • (1870) Proc. R. Soc. Edin. , vol.7 , pp. 506-511
    • Fraser, T.R.1
  • 22
    • 0000166289 scopus 로고
    • Treatment of enzyme kinetic data. I. The effect of modifiers on the kinetic parameters of single substrate enzymes
    • Frieden C. Treatment of enzyme kinetic data. I. The effect of modifiers on the kinetic parameters of single substrate enzymes. J. Biol. Chem. 239 (1964) 3522-3531
    • (1964) J. Biol. Chem. , vol.239 , pp. 3522-3531
    • Frieden, C.1
  • 23
    • 0029801953 scopus 로고    scopus 로고
    • Human myeloblastin (leukocyte proteinase 3): reactions with substrates, inactivators and activators in comparison with leukocyte elastase
    • Früh H., Kostoulas G., Michel B.A., and Baici A. Human myeloblastin (leukocyte proteinase 3): reactions with substrates, inactivators and activators in comparison with leukocyte elastase. Biol. Chem. 377 (1996) 579-586
    • (1996) Biol. Chem. , vol.377 , pp. 579-586
    • Früh, H.1    Kostoulas, G.2    Michel, B.A.3    Baici, A.4
  • 24
    • 34247845704 scopus 로고    scopus 로고
    • Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease
    • Gao W.Q., Anderson P.J., Majerus E.M., Tuley E.A., and Sadler J.E. Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease. Proc. Natl. Acad. Sci. USA 103 (2006) 19099-19104
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19099-19104
    • Gao, W.Q.1    Anderson, P.J.2    Majerus, E.M.3    Tuley, E.A.4    Sadler, J.E.5
  • 25
    • 0017601194 scopus 로고
    • Evidence for allosteric NADH regulation of acinetobacter a-oxoglutarate dehydrogenase from multiple-inhibition studies
    • 10.1016/0006-291X(77)90627-1
    • Hall E.R., and Weitzman P.D.J. Evidence for allosteric NADH regulation of acinetobacter a-oxoglutarate dehydrogenase from multiple-inhibition studies. Biochem. Biophys. Res. Commun. 74 (1977) 1613-1617 10.1016/0006-291X(77)90627-1
    • (1977) Biochem. Biophys. Res. Commun. , vol.74 , pp. 1613-1617
    • Hall, E.R.1    Weitzman, P.D.J.2
  • 26
    • 84988074926 scopus 로고
    • Symbolism and terminology in enzyme kinetics. Recommendations 1981
    • International Union of Biochemistry
    • International Union of Biochemistry. Symbolism and terminology in enzyme kinetics. Recommendations 1981. Eur. J. Biochem. 128 (1982) 281-291
    • (1982) Eur. J. Biochem. , vol.128 , pp. 281-291
  • 27
    • 0014125588 scopus 로고
    • The liberator
    • 10.1016/0022-5193(67)90060-4
    • Keleti T. The liberator. J. Theor. Biol. 16 (1967) 337-355 10.1016/0022-5193(67)90060-4
    • (1967) J. Theor. Biol. , vol.16 , pp. 337-355
    • Keleti, T.1
  • 28
    • 0004835441 scopus 로고
    • The system of double inhibitions
    • 10.1016/0025-5564(71)90016-2
    • Keleti T., and Fajszi C. The system of double inhibitions. Math. Biosci. 12 (1971) 197-215 10.1016/0025-5564(71)90016-2
    • (1971) Math. Biosci. , vol.12 , pp. 197-215
    • Keleti, T.1    Fajszi, C.2
  • 29
    • 66149155033 scopus 로고    scopus 로고
    • A novel, species-specific class of uncompetitive inhibitors of g-glutamyl transpeptidase
    • King J.B., West M.B., Cook P.F., and Hanigan M.H. A novel, species-specific class of uncompetitive inhibitors of g-glutamyl transpeptidase. J. Biol. Chem. 284 (2009) 9059-9065
    • (2009) J. Biol. Chem. , vol.284 , pp. 9059-9065
    • King, J.B.1    West, M.B.2    Cook, P.F.3    Hanigan, M.H.4
  • 30
    • 0344110519 scopus 로고    scopus 로고
    • Electrostatic interactions between human leukocyte elastase and sulfated glycosaminoglycans: physiological implications
    • Kostoulas G., Hörler D., Naggi A., Casu B., and Baici A. Electrostatic interactions between human leukocyte elastase and sulfated glycosaminoglycans: physiological implications. Biol. Chem. 378 (1997) 1481-1489
    • (1997) Biol. Chem. , vol.378 , pp. 1481-1489
    • Kostoulas, G.1    Hörler, D.2    Naggi, A.3    Casu, B.4    Baici, A.5
  • 31
    • 0024548488 scopus 로고
    • Double inhibition of l-threonine dehydratase by aminothiols
    • 10.1016/0167-4838(89)90061-7
    • Leoncini R., Pagani R., Marinello E., and Keleti T. Double inhibition of l-threonine dehydratase by aminothiols. Biochim. Biophys. Acta 994 (1989) 52-58 10.1016/0167-4838(89)90061-7
    • (1989) Biochim. Biophys. Acta , vol.994 , pp. 52-58
    • Leoncini, R.1    Pagani, R.2    Marinello, E.3    Keleti, T.4
  • 32
    • 0018653269 scopus 로고
    • Double inhibition of d-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase
    • Lien L.V., Ecsedi G., and Keleti T. Double inhibition of d-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase. Acta Biochim. Biophys. Acad. Sci. Hung. 14 (1979) 11-17
    • (1979) Acta Biochim. Biophys. Acad. Sci. Hung. , vol.14 , pp. 11-17
    • Lien, L.V.1    Ecsedi, G.2    Keleti, T.3
  • 33
    • 0018662591 scopus 로고
    • pH and temperature dependence of the double inhibition of d-glyceraldehyde-3-phosphate dehydrogenase by ATP and quinaldate
    • Lien L.V., Koubakouenda H., and Keleti T. pH and temperature dependence of the double inhibition of d-glyceraldehyde-3-phosphate dehydrogenase by ATP and quinaldate. Acta Biochim. Biophys. Acad. Sci. Hung. 14 (1979) 19-24
    • (1979) Acta Biochim. Biophys. Acad. Sci. Hung. , vol.14 , pp. 19-24
    • Lien, L.V.1    Koubakouenda, H.2    Keleti, T.3
  • 34
    • 0015443845 scopus 로고
    • Enzymatic catalysis and the transition state theory of reaction rates: transition state analogs
    • Lienhard G.E. Enzymatic catalysis and the transition state theory of reaction rates: transition state analogs. Cold Spring Harbor Symp. Quant. Biol. 36 (1971) 45-51
    • (1971) Cold Spring Harbor Symp. Quant. Biol. , vol.36 , pp. 45-51
    • Lienhard, G.E.1
  • 35
    • 34250958584 scopus 로고
    • Über Kombinationswirkungen. I. Mitteilung: Hilfsmittel der Fragestellung
    • Loewe S., and Muischnek H. Über Kombinationswirkungen. I. Mitteilung: Hilfsmittel der Fragestellung. Arch. Exp. Pathol. Pharmakol. 114 (1926) 313-326
    • (1926) Arch. Exp. Pathol. Pharmakol. , vol.114 , pp. 313-326
    • Loewe, S.1    Muischnek, H.2
  • 36
    • 0000705433 scopus 로고
    • Studies on active center of trypsin. The binding of amidines and guanidines as models of the substrate side chain
    • Mares-Guia M., and Shaw E. Studies on active center of trypsin. The binding of amidines and guanidines as models of the substrate side chain. J. Biol. Chem. 240 (1965) 1579-1585
    • (1965) J. Biol. Chem. , vol.240 , pp. 1579-1585
    • Mares-Guia, M.1    Shaw, E.2
  • 38
    • 0019530481 scopus 로고
    • The measure of synergy in enzymatic regulation. A general coefficient
    • 10.1016/S0300-9084(81)80173-3
    • Mazat F., Langla J., and Mazat J.P. The measure of synergy in enzymatic regulation. A general coefficient. Biochimie 63 (1981) 107-111 10.1016/S0300-9084(81)80173-3
    • (1981) Biochimie , vol.63 , pp. 107-111
    • Mazat, F.1    Langla, J.2    Mazat, J.P.3
  • 39
    • 0020797581 scopus 로고
    • A new plot for multiple enzyme inhibition
    • Palatini P. A new plot for multiple enzyme inhibition. Biochem. Int. 7 (1983) 247-254
    • (1983) Biochem. Int. , vol.7 , pp. 247-254
    • Palatini, P.1
  • 40
    • 0020519113 scopus 로고
    • The interaction between full and partial inhibitors acting on a single enzyme. A theoretical analysis
    • Palatini P. The interaction between full and partial inhibitors acting on a single enzyme. A theoretical analysis. Mol. Pharmacol. 24 (1983) 30-41
    • (1983) Mol. Pharmacol. , vol.24 , pp. 30-41
    • Palatini, P.1
  • 41
    • 0014783489 scopus 로고
    • Complexes of liver alcohol dehydrogenase. Further studies on the rate of inactivation
    • Reynolds C.H., Morris D.L., and McKinley-McKee J.S. Complexes of liver alcohol dehydrogenase. Further studies on the rate of inactivation. Eur. J. Biochem. 14 (1970) 14-26
    • (1970) Eur. J. Biochem. , vol.14 , pp. 14-26
    • Reynolds, C.H.1    Morris, D.L.2    McKinley-McKee, J.S.3
  • 44
    • 0015987113 scopus 로고
    • Steady-state kinetics of rabbit-intestinal sucrase. Kinetic mechanism, Na+ activation, inhibition by tris(hydroxymethyl)aminomethane at the glucose subsite
    • Semenza G., and von Balthazar A.K. Steady-state kinetics of rabbit-intestinal sucrase. Kinetic mechanism, Na+ activation, inhibition by tris(hydroxymethyl)aminomethane at the glucose subsite. Eur. J. Biochem. 41 (1974) 149-162
    • (1974) Eur. J. Biochem. , vol.41 , pp. 149-162
    • Semenza, G.1    von Balthazar, A.K.2
  • 45
    • 84958688743 scopus 로고
    • The effect of fluoride on the succinic oxidase system
    • Slater E.C., and Bonner Jr. W.D. The effect of fluoride on the succinic oxidase system. Biochem. J. 52 (1952) 185-196
    • (1952) Biochem. J. , vol.52 , pp. 185-196
    • Slater, E.C.1    Bonner Jr., W.D.2
  • 46
    • 0020103862 scopus 로고
    • Subsite mapping of enzymes. Double inhibition studies
    • Thoma J.A., and Crook C. Subsite mapping of enzymes. Double inhibition studies. Eur. J. Biochem. 122 (1982) 613-618
    • (1982) Eur. J. Biochem. , vol.122 , pp. 613-618
    • Thoma, J.A.1    Crook, C.2
  • 47
    • 0026532611 scopus 로고
    • In defence of the general validity of the Cha method of deriving rate equations. The importance of explicit recognition of the thermodynamic box in enzyme kinetics
    • Topham C.M., and Brocklehurst K. In defence of the general validity of the Cha method of deriving rate equations. The importance of explicit recognition of the thermodynamic box in enzyme kinetics. Biochem. J. 282 (1992) 261-265
    • (1992) Biochem. J. , vol.282 , pp. 261-265
    • Topham, C.M.1    Brocklehurst, K.2
  • 49
    • 4243801302 scopus 로고
    • Mechanism of inhibition of d-amino acid oxidase. III. Kinetic analysis of the behaviour of chloramphenicol, streptomycin and penicillin in their competition with flavin-adenine dinucleotide
    • 10.1016/0006-3002(60)90815-5
    • Yagi K., and Ozawa T. Mechanism of inhibition of d-amino acid oxidase. III. Kinetic analysis of the behaviour of chloramphenicol, streptomycin and penicillin in their competition with flavin-adenine dinucleotide. Biochim. Biophys. Acta 39 (1960) 304-310 10.1016/0006-3002(60)90815-5
    • (1960) Biochim. Biophys. Acta , vol.39 , pp. 304-310
    • Yagi, K.1    Ozawa, T.2
  • 50
    • 0000096350 scopus 로고
    • Complex formation of apo-enzyme, coenzyme and substrate of d-amino acid oxidase. I. Kinetic analysis using indicators
    • 10.1016/0006-3002(60)90167-0
    • Yagi K., and Ozawa T. Complex formation of apo-enzyme, coenzyme and substrate of d-amino acid oxidase. I. Kinetic analysis using indicators. Biochim. Biophys. Acta 42 (1960) 381-387 10.1016/0006-3002(60)90167-0
    • (1960) Biochim. Biophys. Acta , vol.42 , pp. 381-387
    • Yagi, K.1    Ozawa, T.2
  • 51
    • 0000957077 scopus 로고
    • Studies on liver alcohol dehydrogenase complexes. III. Multiple inhibition kinetics in the presence of two competitive inhibitors
    • 10.1016/0003-9861(64)90184-5
    • Yonetani T., and Theorell H. Studies on liver alcohol dehydrogenase complexes. III. Multiple inhibition kinetics in the presence of two competitive inhibitors. Arch. Biochem. Biophys. 106 (1964) 243-251 10.1016/0003-9861(64)90184-5
    • (1964) Arch. Biochem. Biophys. , vol.106 , pp. 243-251
    • Yonetani, T.1    Theorell, H.2


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