메뉴 건너뛰기




Volumn 271, Issue 1, 2004, Pages 220-234

Damped oscillatory hysteretic behaviour of butyrylcholinesterase with benzoylcholine as substrate

Author keywords

Benzoylcholine; Butyrylcholinesterase; Damped oscillations; Hysteresis; Slow conformational change

Indexed keywords

BENZOYLCHOLINE; CHOLINESTERASE; MUTANT PROTEIN; PHOSPHATE; THIOCHOLINE;

EID: 1642458106     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03924.x     Document Type: Article
Times cited : (37)

References (63)
  • 3
    • 0037012468 scopus 로고    scopus 로고
    • Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine
    • Mesulam, M.M., Guillozet, A., Shaw, P., Levey, A., Duysen, E.G. & Lockridge, O. (2002) Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine. Neuroscience 110, 627-639.
    • (2002) Neuroscience , vol.110 , pp. 627-639
    • Mesulam, M.M.1    Guillozet, A.2    Shaw, P.3    Levey, A.4    Duysen, E.G.5    Lockridge, O.6
  • 4
    • 0025294717 scopus 로고
    • Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine
    • Lockridge, O. (1990) Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol. Ther. 47, 35-60.
    • (1990) Pharmacol. Ther. , vol.47 , pp. 35-60
    • Lockridge, O.1
  • 5
    • 0347647566 scopus 로고    scopus 로고
    • Nerve agents bioscavengers: Protection with reduced behavioral effects
    • Cesaroli, D.M. & Lenz, D.L. (2002) Nerve agents bioscavengers: protection with reduced behavioral effects. Milit. Psychol. 14, 121-143.
    • (2002) Milit. Psychol. , vol.14 , pp. 121-143
    • Cesaroli, D.M.1    Lenz, D.L.2
  • 6
    • 0036164151 scopus 로고    scopus 로고
    • Engineering of a monomeric and low-glycosylated form of human butyrylcholinesterase: Expression, purification, characterization and crystallization
    • Nachon, F., Nicolet, Y., Viguié, N., Masson, P., Fontecilla-Camps, J.-C. & Lockridge O. (2002) Engineering of a monomeric and low-glycosylated form of human butyrylcholinesterase: expression, purification, characterization and crystallization. Eur. J. Biochem. 262, 630-637.
    • (2002) Eur. J. Biochem. , vol.262 , pp. 630-637
    • Nachon, F.1    Nicolet, Y.2    Viguié, N.3    Masson, P.4    Fontecilla-Camps, J.-C.5    Lockridge, O.6
  • 7
    • 0142039868 scopus 로고    scopus 로고
    • Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
    • Nicolet, Y., Lockridge, O., Masson, P., Fontecilla-Camps, J.-C. & Nachon, F. (2003) Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J. Biol. Chem. 278, 41141-41147.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41141-41147
    • Nicolet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.-C.4    Nachon, F.5
  • 8
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica; a prototypic acetylcholine-binding protein
    • Sussman, J.L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L. & Silman, I. (1991) Atomic structure of acetylcholinesterase from Torpedo californica; a prototypic acetylcholine-binding protein. Science 253, 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 11
  • 12
    • 0038219567 scopus 로고    scopus 로고
    • Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate
    • Johnson, J.L., Cusack, B., Davies, M.P., Fauq, A. & Rosenberry, T.L. (2003) Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate. Biochemistry 42, 5438-5452.
    • (2003) Biochemistry , vol.42 , pp. 5438-5452
    • Johnson, J.L.1    Cusack, B.2    Davies, M.P.3    Fauq, A.4    Rosenberry, T.L.5
  • 13
    • 0032946621 scopus 로고    scopus 로고
    • Polyol-induced activation by excess substrate of the D70G butyrylcholinesterase mutant
    • Levitsky, V., Xie, W., Froment, M.-T., Lockridge, O. & Masson, P. (1999) Polyol-induced activation by excess substrate of the D70G butyrylcholinesterase mutant. Biochim. Biophys. Acta 1429, 422-430.
    • (1999) Biochim. Biophys. Acta , vol.1429 , pp. 422-430
    • Levitsky, V.1    Xie, W.2    Froment, M.-T.3    Lockridge, O.4    Masson, P.5
  • 14
    • 0001753330 scopus 로고
    • Acetylcholinesterase: Enthalpies and entropies of activation
    • Wilson, I. & Cabib, E. (1956) Acetylcholinesterase: enthalpies and entropies of activation. J. Am. Chem. Soc. 78, 202-207.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 202-207
    • Wilson, I.1    Cabib, E.2
  • 15
    • 0023241821 scopus 로고
    • Kinetic evidence for thermally induced conformational change of butyrylcholinesterase
    • Ferro, A. & Masson, P. (1987) Kinetic evidence for thermally induced conformational change of butyrylcholinesterase. Biochim. Biophys. Acta 916, 193-199.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 193-199
    • Ferro, A.1    Masson, P.2
  • 16
    • 0037013985 scopus 로고    scopus 로고
    • Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: Analysis of volume changes upon reaction and hysteretic behavior
    • Masson, P., Froment, M.T., Fort, S., Ribes, F., Bee, N., Balny, C. & Schopfer, L.M. (2002) Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: analysis of volume changes upon reaction and hysteretic behavior. Biochim. Biophys. Acta 1597, 229-243.
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 229-243
    • Masson, P.1    Froment, M.T.2    Fort, S.3    Ribes, F.4    Bee, N.5    Balny, C.6    Schopfer, L.M.7
  • 17
    • 0018401599 scopus 로고
    • Slow transitions and hysteretic behavior in enzymes
    • Frieden, C. (1979) Slow transitions and hysteretic behavior in enzymes. Annu. Rev. Biochem. 48, 471-489.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 471-489
    • Frieden, C.1
  • 19
    • 0017196750 scopus 로고
    • The theoretical analysis of kinetic behaviour of 'hysteretic' allosteric enzymes
    • Kurganov, B.I., Dorozhko, A.I., Kagan, Z.S. & Yakovlev, V.A. (1976) The theoretical analysis of kinetic behaviour of 'hysteretic' allosteric enzymes. J. Theor. Biol. 60, 247-269.
    • (1976) J. Theor. Biol. , vol.60 , pp. 247-269
    • Kurganov, B.I.1    Dorozhko, A.I.2    Kagan, Z.S.3    Yakovlev, V.A.4
  • 20
    • 0023687406 scopus 로고
    • Stability of butyrylcholinesterase: Thermal inactivation in water and deuterium oxide
    • Masson, P. & Laurentie, M. (1988) Stability of butyrylcholinesterase: thermal inactivation in water and deuterium oxide. Biochim. Biophys. Acta 957, 111-121.
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 111-121
    • Masson, P.1    Laurentie, M.2
  • 21
    • 0027273738 scopus 로고
    • Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant
    • Masson, P., Adkins, S., Gouet, P. & Lockridge, O. (1993) Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant. J. Biol. Chem. 268, 14329-14341.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14329-14341
    • Masson, P.1    Adkins, S.2    Gouet, P.3    Lockridge, O.4
  • 23
    • 0017886921 scopus 로고
    • Functional consequences of ligand-dependent conformational changes in trypsin-solubilized and in membrane particle constrained-acetylcholinesterase
    • Pattison, S. & Bernhard, S. (1978) Functional consequences of ligand-dependent conformational changes in trypsin-solubilized and in membrane particle constrained-acetylcholinesterase. Proc. Natl Acad. Sci. USA 75, 3613-3617.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 3613-3617
    • Pattison, S.1    Bernhard, S.2
  • 24
    • 0018784005 scopus 로고
    • Kinetics of association between bisquaternary ammonium ligands and acetylcholinesterase. Evidence for two conformational states of the enzyme from stopped-flow measurements of fluorescence
    • Bolger, M.B. & Taylor, P. (1979) Kinetics of association between bisquaternary ammonium ligands and acetylcholinesterase. Evidence for two conformational states of the enzyme from stopped-flow measurements of fluorescence. Biochemistry 18, 3622-3629.
    • (1979) Biochemistry , vol.18 , pp. 3622-3629
    • Bolger, M.B.1    Taylor, P.2
  • 25
    • 1642516846 scopus 로고    scopus 로고
    • Hysteretic behavior of butyrylcholinesterase: Kinetic curiosity or catalytically and physiologically significant
    • Pucon, Chile, November 8-12, 2002. FONDAP-Biomedicina, Santiago de Chile
    • Masson, P., Froment, M-T., Nachon, F., Lockridge, O. & Schopfer, L.M. (2004) Hysteretic behavior of butyrylcholinesterase: kinetic curiosity or catalytically and physiologically significant. Proceedings of the 7th International Meeting on Cholinesterases, Pucon, Chile, November 8-12, 2002. FONDAP-Biomedicina, Santiago de Chile.
    • (2004) Proceedings of the 7th International Meeting on Cholinesterases
    • Masson, P.1    Froment, M.-T.2    Nachon, F.3    Lockridge, O.4    Schopfer, L.M.5
  • 26
    • 0031043533 scopus 로고    scopus 로고
    • Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase
    • Masson, P., Legrand, P., Bartels, C.F., Froment, M.-T., Schopfer, L.M. & Lockridge, L. (1997) Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase. Biochemistry 36, 2266-2277.
    • (1997) Biochemistry , vol.36 , pp. 2266-2277
    • Masson, P.1    Legrand, P.2    Bartels, C.F.3    Froment, M.-T.4    Schopfer, L.M.5    Lockridge, L.6
  • 27
  • 28
    • 0031713093 scopus 로고    scopus 로고
    • Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon
    • Amitai, G., Moorad, D., Adani, R. & Doctor, B.P. (1998) Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon. Biochem. Pharmacol. 56, 293-299.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 293-299
    • Amitai, G.1    Moorad, D.2    Adani, R.3    Doctor, B.P.4
  • 29
    • 0020608395 scopus 로고
    • Analysis of cyclic enzyme reaction schemes by the graph-theoretic method
    • Goldstein, B.N. (1983) Analysis of cyclic enzyme reaction schemes by the graph-theoretic method. J. Theor. Biol. 103, 247-264.
    • (1983) J. Theor. Biol. , vol.103 , pp. 247-264
    • Goldstein, B.N.1
  • 30
    • 0023190458 scopus 로고
    • Hormonal regulation of 6-phosphofructo-2-kinase/fructose-2,6- biphosphatase: Kinetic models
    • Goldstein, B.N. & Ivanova, A.N. (1987) Hormonal regulation of 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase: kinetic models. FEBS Lett. 217, 212-215.
    • (1987) FEBS Lett. , vol.217 , pp. 212-215
    • Goldstein, B.N.1    Ivanova, A.N.2
  • 31
    • 0032944436 scopus 로고    scopus 로고
    • An improved cocaine hydrolase: The A328Y mutant of human butyrylcholinesterase is 4-fold more efficient
    • Xie, W., Varkey-Altamirano, C. Bartels, C.F., Speirs, R.J., Cashman, J.R. & Lockridge, O. (1999) An improved cocaine hydrolase: the A328Y mutant of human butyrylcholinesterase is 4-fold more efficient. Mol. Pharmacol. 55, 83-91.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 83-91
    • Xie, W.1    Varkey-Altamirano, C.2    Bartels, C.F.3    Speirs, R.J.4    Cashman, J.R.5    Lockridge, O.6
  • 32
    • 0031868426 scopus 로고    scopus 로고
    • Cocaine benzoyl thioester: Synthesis, kinetics of base hydrolysis, and application to the assay of cocaine esterases
    • Cashman, J.R., Berkman, C.E., Underiner, G., Kolly, C.A. & Hunter, A.D. (1998) Cocaine benzoyl thioester: synthesis, kinetics of base hydrolysis, and application to the assay of cocaine esterases. Chem. Res. Toxicol. 11, 895-901.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 895-901
    • Cashman, J.R.1    Berkman, C.E.2    Underiner, G.3    Kolly, C.A.4    Hunter, A.D.5
  • 33
    • 0001424293 scopus 로고
    • The influence of pH on the hydrolysis of benzoylcholine by pseudocholinesterase of human plasma
    • Kalow, W. (1964) The influence of pH on the hydrolysis of benzoylcholine by pseudocholinesterase of human plasma. Can. J. Physiol. Pharmacol. 42, 161-168.
    • (1964) Can. J. Physiol. Pharmacol. , vol.42 , pp. 161-168
    • Kalow, W.1
  • 34
    • 0013916456 scopus 로고
    • Chemical structure and function of the active center of acetylcholinesterase
    • Krupka, R.M. (1966) Chemical structure and function of the active center of acetylcholinesterase. Biochemistry 6, 1988-1997.
    • (1966) Biochemistry , vol.6 , pp. 1988-1997
    • Krupka, R.M.1
  • 35
    • 0021126688 scopus 로고
    • Direct determination of acetylenzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine
    • Froede, H.C. & Wilson, I.B. (1984) Direct determination of acetylenzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine. J. Biol. Chem. 259, 11010-11013.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11010-11013
    • Froede, H.C.1    Wilson, I.B.2
  • 37
    • 0029665127 scopus 로고    scopus 로고
    • Asp70 in the peripheral anionic site of human butyrylcholinesterase
    • Masson, P., Froment, M.-T., Bartels, C.F. & Lockridge, O. (1996) Asp70 in the peripheral anionic site of human butyrylcholinesterase. Eur. J. Biochem. 235, 36-48.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 36-48
    • Masson, P.1    Froment, M.-T.2    Bartels, C.F.3    Lockridge, O.4
  • 38
    • 0014959666 scopus 로고
    • Hydrolysis of electronically and sterically defined substrates of acetylcholinesterase
    • Hillman, G.R. & Mautner, H.G. (1970) Hydrolysis of electronically and sterically defined substrates of acetylcholinesterase. Biochemistry 9, 2633-2638.
    • (1970) Biochemistry , vol.9 , pp. 2633-2638
    • Hillman, G.R.1    Mautner, H.G.2
  • 39
    • 0016163587 scopus 로고
    • The hydrolysis of choline and thiocholine esters by cholinesterases
    • Bretskin, A.P., Zhukovskii, Y.G. & Sipenkova, T.M. (1974) The hydrolysis of choline and thiocholine esters by cholinesterases. Biochemistry (Moscow) 39, 13-18.
    • (1974) Biochemistry (Moscow) , vol.39 , pp. 13-18
    • Bretskin, A.P.1    Zhukovskii, Y.G.2    Sipenkova, T.M.3
  • 42
    • 0036226101 scopus 로고    scopus 로고
    • Properties of water molecules in the active site gorge of acetylcholinesterase from computer simulation
    • Henchman, R.H., Tsai, K., Shen, T. & McCammon, A. (2002) Properties of water molecules in the active site gorge of acetylcholinesterase from computer simulation. Biophys. J. 82, 2671-2682.
    • (2002) Biophys. J. , vol.82 , pp. 2671-2682
    • Henchman, R.H.1    Tsai, K.2    Shen, T.3    McCammon, A.4
  • 43
    • 0036707992 scopus 로고    scopus 로고
    • Structural and dynamic properties of water around acetylcholinesterase
    • Henchman, R.H. & McCammon, A.C. (2002) Structural and dynamic properties of water around acetylcholinesterase. Protein Sci. 11, 2080-2090.
    • (2002) Protein Sci. , vol.11 , pp. 2080-2090
    • Henchman, R.H.1    McCammon, A.C.2
  • 44
    • 2442769298 scopus 로고    scopus 로고
    • Hydration changes during the aging of phosphorylated human butyrylcholinesterase: Importance of residues aspartate-70 and glutamate-197 in the water network as probed by hydrostatic and osmotic pressures
    • Masson, P., Cléry, C., Guerra, P., Redslob, A., Albaret, C. & Fortier, P.-L. (1999) Hydration changes during the aging of phosphorylated human butyrylcholinesterase: importance of residues aspartate-70 and glutamate-197 in the water network as probed by hydrostatic and osmotic pressures. Biochem. J. 343, 361-369.
    • (1999) Biochem. J. , vol.343 , pp. 361-369
    • Masson, P.1    Cléry, C.2    Guerra, P.3    Redslob, A.4    Albaret, C.5    Fortier, P.-L.6
  • 45
    • 0025202704 scopus 로고
    • Conformational plasticity of butyrylcholinesterase as revealed by high pressure experiments
    • Masson, P. & Balny, C. (1990) Conformational plasticity of butyrylcholinesterase as revealed by high pressure experiments. Biochim. Biophys. Acta 1041, 223-231.
    • (1990) Biochim. Biophys. Acta , vol.1041 , pp. 223-231
    • Masson, P.1    Balny, C.2
  • 46
    • 0015173025 scopus 로고
    • Oscillations phenomena in biochemistry
    • Hess, B. & Boiteux, A. (1971) Oscillations phenomena in biochemistry. Annu. Rev. Biochem. 40, 237-258.
    • (1971) Annu. Rev. Biochem. , vol.40 , pp. 237-258
    • Hess, B.1    Boiteux, A.2
  • 47
    • 0037526560 scopus 로고    scopus 로고
    • Implications of enzyme kinetics
    • McDonald, A.G. (2003) Implications of enzyme kinetics. Biochem. Soc. Trans. 31, 719-722.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 719-722
    • McDonald, A.G.1
  • 48
    • 0014024607 scopus 로고
    • Highly damped oscillations in a peroxidase-like enzyme reaction
    • Strickland, E.H. & Ackerman, E. (1966) Highly damped oscillations in a peroxidase-like enzyme reaction. Nature 209, 405-406.
    • (1966) Nature , vol.209 , pp. 405-406
    • Strickland, E.H.1    Ackerman, E.2
  • 49
    • 0021403583 scopus 로고
    • pH modulation of transient state kinetics of enzymes. I. Simple theoretical models
    • Ricard, J. & Crasnier, M. (1984) pH modulation of transient state kinetics of enzymes. I. Simple theoretical models. Biophys. Chem. 19, 85-91.
    • (1984) Biophys. Chem. , vol.19 , pp. 85-91
    • Ricard, J.1    Crasnier, M.2
  • 50
    • 0024818508 scopus 로고
    • A theoretical treatment of damped oscillations in the transient state kinetics of single-enzyme reactions
    • Ryde-Petterson, U. (1989) A theoretical treatment of damped oscillations in the transient state kinetics of single-enzyme reactions. Eur. J. Biochem. 186, 145-148.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 145-148
    • Ryde-Petterson, U.1
  • 51
    • 0032556477 scopus 로고    scopus 로고
    • Slowly reverting enzyme inactivation: A mechanism for generating Ion-lived damped oscillations
    • Roussel, M.R. (1998) Slowly reverting enzyme inactivation: a mechanism for generating Ion-lived damped oscillations. J. Theor. Biol. 195, 233-244.
    • (1998) J. Theor. Biol. , vol.195 , pp. 233-244
    • Roussel, M.R.1
  • 52
    • 1642476207 scopus 로고
    • pH modulation of transient state kinetics of enzymes. II. Transient state kinetics of plant cell wall acid phosphatase
    • Crasnier, M. & Ricard, J. (1984) pH modulation of transient state kinetics of enzymes. II. Transient state kinetics of plant cell wall acid phosphatase. Biophys. Chem. 19, 93-98.
    • (1984) Biophys. Chem. , vol.19 , pp. 93-98
    • Crasnier, M.1    Ricard, J.2
  • 53
    • 0032562130 scopus 로고    scopus 로고
    • The role of naturally occurring phenols in inducing oscillations in the peroxidase-oxidase reaction
    • Hauser, M.J.B. & Olsen, L.F. (1998) The role of naturally occurring phenols in inducing oscillations in the peroxidase-oxidase reaction. Biochemistry 37, 2458-2469.
    • (1998) Biochemistry , vol.37 , pp. 2458-2469
    • Hauser, M.J.B.1    Olsen, L.F.2
  • 56
    • 0023065955 scopus 로고
    • Oscillatory phenomena in immobilized enzyme systems
    • Hervagault, J.F. & Thomas, D. (1987) Oscillatory phenomena in immobilized enzyme systems. Methods Enzymol. 135, 554-569.
    • (1987) Methods Enzymol. , vol.135 , pp. 554-569
    • Hervagault, J.F.1    Thomas, D.2
  • 57
    • 0037178110 scopus 로고    scopus 로고
    • The solute-solvent system: Solvent constraints on the conformational dynamics of acetylcholine
    • Vistoli, G., Pedretti, A., Villa, L. & Testa, B. (2002) The solute-solvent system: solvent constraints on the conformational dynamics of acetylcholine. J. Am. Chem. Soc. 124, 7472-7480.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7472-7480
    • Vistoli, G.1    Pedretti, A.2    Villa, L.3    Testa, B.4
  • 60
    • 0028069358 scopus 로고
    • Site-directed mutagenesis of active site residues reveals plasticity of human butyrylcholinesterase in substrate and inhibitor interactions
    • Gnatt, A., Loewenstein, Y., Yaron, A., Schwarz, M. & Soreq, H. (1994) Site-directed mutagenesis of active site residues reveals plasticity of human butyrylcholinesterase in substrate and inhibitor interactions. J. Neurochem. 62, 749-775.
    • (1994) J. Neurochem. , vol.62 , pp. 749-775
    • Gnatt, A.1    Loewenstein, Y.2    Yaron, A.3    Schwarz, M.4    Soreq, H.5
  • 62
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution: A 60-year-old hypothesis revisited
    • James, L.C. & Tawfik, D.S. (2003) Conformational diversity and protein evolution: a 60-year-old hypothesis revisited. Trends Biochem. Sci. 28, 361-368.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 63
    • 0015968641 scopus 로고
    • Transient-phase kinetics of α-chymotrypsin and other enzyme systems
    • Maguire, R.J., Hijazi, N.H. & Laidler, K.J. (1974) Transient-phase kinetics of α-chymotrypsin and other enzyme systems. Biochim. Biophys. Acta 341, 1-14.
    • (1974) Biochim. Biophys. Acta , vol.341 , pp. 1-14
    • Maguire, R.J.1    Hijazi, N.H.2    Laidler, K.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.