메뉴 건너뛰기




Volumn , Issue , 2008, Pages 1-301

Enzyme Kinetics: Principles and Methods: Second Edition

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84889411295     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527622023     Document Type: Book
Times cited : (136)

References (245)
  • 1
    • 33747775622 scopus 로고    scopus 로고
    • Practical Enzymology
    • Wiley-VCH, Weinheim
    • Bisswanger, H. (2004) Practical Enzymology, Wiley-VCH, Weinheim.
    • (2004)
    • Bisswanger, H.1
  • 2
    • 0004086386 scopus 로고
    • Principles of Enzyme Kinetics
    • Butterworth, London, Boston
    • Cornish-Bowden, A. (1976) Principles of Enzyme Kinetics, Butterworth, London, Boston.
    • (1976)
    • Cornish-Bowden, A.1
  • 3
    • 0004205267 scopus 로고    scopus 로고
    • Fundamentals of Enzyme Kinetics
    • 3rd edn, Portland Press Ltd. London
    • Cornish-Bowden, A. (2004) Fundamentals of Enzyme Kinetics, 3rd edn, Portland Press Ltd. London.
    • (2004)
    • Cornish-Bowden, A.1
  • 4
    • 0003743975 scopus 로고
    • Enzyme Kinetics
    • IRL Press, Oxford
    • Cornish-Bowden, A., Wharton, C.W. (1988) Enzyme Kinetics, IRL Press, Oxford.
    • (1988)
    • Cornish-Bowden, A.1    Wharton, C.W.2
  • 5
    • 0004262303 scopus 로고
    • Enzymes
    • Academic Press, New York
    • Dixon, M., Webb, E. C. (1979) Enzymes, Academic Press, New York.
    • (1979)
    • Dixon, M.1    Webb, E.C.2
  • 6
    • 0004197083 scopus 로고
    • Biothermodynamics
    • J. Wiley & Sons, New York
    • Edsall, J.T., Gutfreund, H. (1983) Biothermodynamics, J. Wiley & Sons, New York.
    • (1983)
    • Edsall, J.T.1    Gutfreund, H.2
  • 8
    • 0003818741 scopus 로고    scopus 로고
    • Enzymology Labfax
    • Academic Press, New York
    • Engel, P. C. (1996) Enzymology Labfax, Academic Press, New York.
    • (1996)
    • Engel, P.C.1
  • 9
    • 0003481596 scopus 로고
    • Enzyme Structure and Mechanism
    • W.H. Freeman & Co., San Francisco
    • Fersht, A. (1977) Enzyme Structure and Mechanism, W.H. Freeman & Co., San Francisco.
    • (1977)
    • Fersht, A.1
  • 10
    • 84889401721 scopus 로고
    • Initial Rate Kinetics
    • Springer, Berlin
    • Fromm, H.J. (1975) Initial Rate Kinetics, Springer, Berlin.
    • (1975)
    • Fromm, H.J.1
  • 11
    • 0010758416 scopus 로고    scopus 로고
    • Kinetic Analysis of Macromolecules: A Practical Approach
    • Oxford University Press, Oxford
    • Johnson, K. A. (2003) Kinetic Analysis of Macromolecules: A Practical Approach, Oxford University Press, Oxford.
    • (2003)
    • Johnson, K.A.1
  • 12
    • 0004287728 scopus 로고
    • Introduction to Biomolecular Energetics Including Ligand-Receptor Interactions
    • Academic Press, Orlando
    • Klotz, I.M. (1986) Introduction to Biomolecular Energetics Including Ligand-Receptor Interactions, Academic Press, Orlando.
    • (1986)
    • Klotz, I.M.1
  • 13
    • 84889482036 scopus 로고
    • Enzyme Catalysis
    • Kinetics and Substrate Binding, CRC Press, Boca Raton
    • Kuby, S.A. (1991) Enzyme Catalysis, Kinetics and Substrate Binding, CRC Press, Boca Raton.
    • (1991)
    • Kuby, S.A.1
  • 14
    • 0004028668 scopus 로고
    • The Chemical Kinetics of Enzyme Action
    • 2nd edn, Clarendon Press, Oxford
    • Laidler, K. J., Bunting, P. S. (1973) The Chemical Kinetics of Enzyme Action, 2nd edn, Clarendon Press, Oxford.
    • (1973)
    • Laidler, K.J.1    Bunting, P.S.2
  • 15
    • 2542452214 scopus 로고    scopus 로고
    • Comprehensive Enzyme Kinetics
    • Kluwer Academic, Dordrecht
    • Leskovac, V. (2003) Comprehensive Enzyme Kinetics, Kluwer Academic, Dordrecht.
    • (2003)
    • Leskovac, V.1
  • 16
    • 0141489485 scopus 로고    scopus 로고
    • Enzyme Kinetics. A Modern Approach
    • Wiley-Interscience, Hoboken, New Jersey
    • Marangoni, A.G. (2003) Enzyme Kinetics. A Modern Approach, Wiley-Interscience, Hoboken, New Jersey.
    • (2003)
    • Marangoni, A.G.1
  • 17
    • 0010346537 scopus 로고
    • The Chemistry of Enzyme Action
    • Elsevier, Amsterdam
    • Page, M. (Ed.) (1984) The Chemistry of Enzyme Action. New Comprehensive Biochemistry, Vol. 6. Elsevier, Amsterdam.
    • (1984) New Comprehensive Biochemistry , vol.6
    • Page, M.1
  • 18
    • 0004152397 scopus 로고
    • Fundamentals of Enzymology
    • Oxford University Press, Oxford
    • Price, N. C., Stevens, L. (1989) Fundamentals of Enzymology, Oxford University Press, Oxford.
    • (1989)
    • Price, N.C.1    Stevens, L.2
  • 19
    • 84889491403 scopus 로고
    • Enzyme Kinetics and Mechanism
    • Academic Press, New York
    • Purich, D. L. (Ed.) (1982) Enzyme Kinetics and Mechanism, Methods in Enzymology, Vol. 87, Academic Press, New York.
    • (1982) Methods in Enzymology , vol.87
    • Purich, D.L.1
  • 20
    • 0003867860 scopus 로고    scopus 로고
    • Contemporary Enzyme Kinetics and Mechanism
    • Academic Press, New York
    • Purich, D. L. (1996) Contemporary Enzyme Kinetics and Mechanism, Academic Press, New York.
    • (1996)
    • Purich, D.L.1
  • 21
    • 0004209647 scopus 로고    scopus 로고
    • Handbook of Biochemical Kinetics
    • Academic Press, New York
    • Purich, D. L. (1999) Handbook of Biochemical Kinetics, Academic Press, New York.
    • (1999)
    • Purich, D.L.1
  • 22
    • 0003744057 scopus 로고
    • Enzyme Kinetics
    • Cambridge University Press, Cambridge
    • Roberts, D.V. (1977) Enzyme Kinetics, Cambridge University Press, Cambridge.
    • (1977)
    • Roberts, D.V.1
  • 23
    • 0003518480 scopus 로고
    • Enzyme Kinetics
    • J. Wiley & Sons, New York
    • Segel, I.H. (1975) Enzyme Kinetics, J. Wiley & Sons, New York.
    • (1975)
    • Segel, I.H.1
  • 24
    • 10844230260 scopus 로고    scopus 로고
    • Enzyme Kinetics and Mechanisms
    • Kluwer Academic Publishers, Dordrecht, NL, Boston, London
    • Taylor, K.B. (2002) Enzyme Kinetics and Mechanisms, Kluwer Academic Publishers, Dordrecht, NL, Boston, London.
    • (2002)
    • Taylor, K.B.1
  • 25
    • 0346247346 scopus 로고
    • Symbolism and terminology in chemical kinetics
    • Nomenclature rules International Union of Pure and Applied Chemistry
    • Nomenclature rules International Union of Pure and Applied Chemistry (1981) Symbolism and terminology in chemical kinetics, Pure Appl. Chem. 53, 753-771.
    • (1981) Pure Appl. Chem , vol.53 , pp. 753-771
  • 26
    • 84988074926 scopus 로고
    • Symbolism and terminology in enzyme kinetics
    • Nomenclature Committee of the International Union of Biochemistry
    • Nomenclature Committee of the International Union of Biochemistry (1982) Symbolism and terminology in enzyme kinetics, Eur. J. Biochem. 128, 281-291.
    • (1982) Eur. J. Biochem , vol.128 , pp. 281-291
  • 27
    • 0004232671 scopus 로고
    • Random Walks in Biology
    • Princetown University Press, Princetown, New Jersey
    • Berg, H.C. (1983) Random Walks in Biology, Princetown University Press, Princetown, New Jersey.
    • (1983)
    • Berg, H.C.1
  • 28
    • 0021904674 scopus 로고
    • Orientation constraints in diffusion-limited macromolecular association
    • Berg, O.G. (1985) Orientation constraints in diffusion-limited macromolecular association, Biophys. J. 47, 1-14.
    • (1985) Biophys. J. , vol.47 , pp. 1-14
    • Berg, O.G.1
  • 29
    • 0019421683 scopus 로고
    • Gated binding of ligands to protein
    • McCammon, J. A., Northrup, S.H. (1981) Gated binding of ligands to protein, Nature 293, 316-317.
    • (1981) Nature , vol.293 , pp. 316-317
    • McCammon, J.A.1    Northrup, S.H.2
  • 30
    • 0000374395 scopus 로고
    • Effects of diffusion rates in chemical kinetics
    • Noyes, R.M. (1961) Effects of diffusion rates in chemical kinetics, Prog. React. Kinet. 1, 129-160.
    • (1961) Prog. React. Kinet. , vol.1 , pp. 129-160
    • Noyes, R.M.1
  • 31
    • 0001314221 scopus 로고
    • The hemoglobin system. The oxygen dissociation curve of haemoglobin
    • Adair, G.S. (1925) The hemoglobin system. The oxygen dissociation curve of haemoglobin, J. Biol. Chem. 63, 529-545.
    • (1925) J. Biol. Chem. , vol.63 , pp. 529-545
    • Adair, G.S.1
  • 32
    • 0022102432 scopus 로고
    • Ligand-receptor interactions: facts and fantasies
    • Klotz, I.M. (1985) Ligand-receptor interactions: facts and fantasies, Quart. Rev. Biophys. 18, 227-259.
    • (1985) Quart. Rev. Biophys. , vol.18 , pp. 227-259
    • Klotz, I.M.1
  • 33
    • 4043158815 scopus 로고
    • The constitution and fundamental properties of solids and liquids
    • Langmuir, I. (1916) The constitution and fundamental properties of solids and liquids, J. Am. Chem. Soc. 38, 2221-2295.
    • (1916) J. Am. Chem. Soc. , vol.38 , pp. 2221-2295
    • Langmuir, I.1
  • 34
    • 0010758416 scopus 로고    scopus 로고
    • What to do if there is no signal: using competition experiments to determine binding parameters
    • in: Johnson, K. A. Kinetic Analysis of Macromolecules: A Practical Approach, Oxford University Press, Oxford
    • Thomä, N., Goody, R.S. (2003) What to do if there is no signal: using competition experiments to determine binding parameters, in: Johnson, K. A. Kinetic Analysis of Macromolecules: A Practical Approach, Oxford University Press, Oxford.
    • (2003)
    • Thomä, N.1    Goody, R.S.2
  • 35
    • 0020440236 scopus 로고
    • Determination of binding stoichiometry by the continuous variation method: The Job plot
    • Huang, C.Y. (1982) Determination of binding stoichiometry by the continuous variation method: The Job plot, Methods Enzymol. 87, 509-525.
    • (1982) Methods Enzymol. , vol.87 , pp. 509-525
    • Huang, C.Y.1
  • 36
    • 0001511660 scopus 로고
    • Recherches sur la Formation de Complexes Minéraux en Solution, et sur leur Stabilité
    • Job, P. (1928) Recherches sur la Formation de Complexes Minéraux en Solution, et sur leur Stabilité, Ann. Chim. (Paris) 9, 113-203.
    • (1928) Ann. Chim. (Paris) , vol.9 , pp. 113-203
    • Job, P.1
  • 37
    • 0001180450 scopus 로고
    • The application of the law of mass action to binding by proteins. Interaction with calcium
    • Klotz, I.M. (1946) The application of the law of mass action to binding by proteins. Interaction with calcium, Arch. Biochem. 9, 109-117.
    • (1946) Arch. Biochem , vol.9 , pp. 109-117
    • Klotz, I.M.1
  • 38
    • 0014127723 scopus 로고
    • A graphic method for determination and presentation of binding parameters in a complex system
    • Rosenthal, H.R. (1967) A graphic method for determination and presentation of binding parameters in a complex system, Anal. Biochem. 20, 515-532.
    • (1967) Anal. Biochem. , vol.20 , pp. 515-532
    • Rosenthal, H.R.1
  • 39
    • 84969001783 scopus 로고
    • Attractions of proteins for small molecules and ions
    • Scatchard, G. (1949) Attractions of proteins for small molecules and ions, Ann. N.Y. Acad. Sci. 51, 660-672.
    • (1949) Ann. N.Y. Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 40
    • 0004082205 scopus 로고
    • The binding of diphosphopyridine nucleotide by yeast glyceraldehyde-3-phosphate dehydrogenase
    • Stockell, A. (1959) The binding of diphosphopyridine nucleotide by yeast glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem. 234, 1286-1292.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1286-1292
    • Stockell, A.1
  • 41
    • 0015970129 scopus 로고
    • Determination of binding parameters from Scatchard plots. Theoretical and practical considerations
    • Weder, H. G., Schildknecht, J., Lutz, L. A., Kesselring, P. (1974) Determination of binding parameters from Scatchard plots. Theoretical and practical considerations, Eur. J. Biochem. 42, 475-481.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 475-481
    • Weder, H.G.1    Schildknecht, J.2    Lutz, L.A.3    Kesselring, P.4
  • 42
    • 0004212990 scopus 로고    scopus 로고
    • Interfacial Enzyme Kinetics
    • J. Wiley & Sons, Chichester
    • Berg, O.G., Jain, M.K. (2002) Interfacial Enzyme Kinetics, J. Wiley & Sons, Chichester.
    • (2002)
    • Berg, O.G.1    Jain, M.K.2
  • 43
    • 0004673414 scopus 로고
    • Die Sauerstoffaufnahme des genuinen Blutfarbstoffes und des aus dem Blute dargestellten Hämoglobins
    • Bohr, C. (1904) Die Sauerstoffaufnahme des genuinen Blutfarbstoffes und des aus dem Blute dargestellten Hämoglobins, Zentralblatt Physiol. 23, 688-690.
    • (1904) Zentralblatt Physiol. , vol.23 , pp. 688-690
    • Bohr, C.1
  • 44
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux, J.-P., Edelstein, S. J. (2005) Allosteric mechanisms of signal transduction, Science 308, 1424-1428.
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.-P.1    Edelstein, S.J.2
  • 45
    • 0014352175 scopus 로고
    • Negative cooperativity in enzyme action
    • Convay, A., Koshland, D.E. (1968) Negative cooperativity in enzyme action, Biochemistry 7, 4011-4023.
    • (1968) Biochemistry , vol.7 , pp. 4011-4023
    • Convay, A.1    Koshland, D.E.2
  • 46
    • 0017831891 scopus 로고
    • Structural and functional properties of the acetylcholine receptor protein in its purified and membrane-bound states
    • Heidmann, T., Changeux, J.-P. (1978) Structural and functional properties of the acetylcholine receptor protein in its purified and membrane-bound states, Ann. Rev. Biochem. 47, 317-357.
    • (1978) Ann. Rev. Biochem. , vol.47 , pp. 317-357
    • Heidmann, T.1    Changeux, J.-P.2
  • 47
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of molecules of hemoglobin on its dissociation curves
    • Hill, A.V. (1910) The possible effects of the aggregation of molecules of hemoglobin on its dissociation curves, J. Physiol. 40, iv-vii.
    • (1910) J. Physiol , vol.40
    • Hill, A.V.1
  • 48
    • 0008025301 scopus 로고
    • The study of allosteric proteins
    • Janin, J. (1973) The study of allosteric proteins, Prog. Biophys. Mol. Biol. 27, 77-120.
    • (1973) Prog. Biophys. Mol. Biol. , vol.27 , pp. 77-120
    • Janin, J.1
  • 49
    • 0025058563 scopus 로고
    • Aspartate transcarbamoylase: The molecular basis for a concerted allosteric transition
    • Kantrowitz, E. R., Lipscomp, W. N. (1990) Aspartate transcarbamoylase: The molecular basis for a concerted allosteric transition, Trends Biochem. Sci. 15, 53-59.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 53-59
    • Kantrowitz, E.R.1    Lipscomp, W.N.2
  • 50
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland, D.E., Nemethy, G., Filmer, D. (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits, Biochemistry 5, 365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Nemethy, G.2    Filmer, D.3
  • 51
    • 0016898885 scopus 로고
    • The role of negative cooperativity and half-of-thesites reactivity in enzyme regulation
    • Levitzki, A., Koshland, D.E. (1976) The role of negative cooperativity and half-of-thesites reactivity in enzyme regulation, Curr. Top. Cellular Reg. 10, 1-40.
    • (1976) Curr. Top. Cellular Reg. , vol.10 , pp. 1-40
    • Levitzki, A.1    Koshland, D.E.2
  • 52
    • 0002832337 scopus 로고
    • Structure and function of allosteric enzymes
    • Lipscomp, W. N. (1991) Structure and function of allosteric enzymes, Chemtracts-Biochem. Mol. Biol. 2, 1-15.
    • (1991) Chemtracts-Biochem. Mol. Biol. , vol.2 , pp. 1-15
    • Lipscomp, W.N.1
  • 53
    • 78651189765 scopus 로고
    • On the nature of allosteric transition: A plausible model
    • Monod, J., Wyman, J., Changeux, J.-P. (1965) On the nature of allosteric transition: A plausible model, J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 54
    • 0018861067 scopus 로고
    • Cooperativity in enzyme function: Equilibrium and kinetic aspects
    • Neet, K. E. (1980) Cooperativity in enzyme function: Equilibrium and kinetic aspects, Methods Enzymol. 64, 139-192.
    • (1980) Methods Enzymol. , vol.64 , pp. 139-192
    • Neet, K.E.1
  • 55
    • 0000450916 scopus 로고
    • The oxygen equilibrium of hemoglobin and its structural interpretation
    • Pauling, L. (1935) The oxygen equilibrium of hemoglobin and its structural interpretation, Proc. Natl. Acad. Sci. USA 21, 186-191.
    • (1935) Proc. Natl. Acad. Sci. USA , vol.21 , pp. 186-191
    • Pauling, L.1
  • 56
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz, M. (1970) Stereochemistry of cooperative effects in haemoglobin, Nature 228, 726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.1
  • 57
    • 0003557288 scopus 로고
    • Mechanisms of Cooperativity and Allosteric Regulation in Proteins
    • Cambridge University Press, Cambridge
    • Perutz, M. (1990) Mechanisms of Cooperativity and Allosteric Regulation in Proteins, Cambridge University Press, Cambridge.
    • (1990)
    • Perutz, M.1
  • 58
    • 0031859481 scopus 로고    scopus 로고
    • Annu. Rev. Biophys. Biomol. Struct
    • Perutz, M., Wilkinson, A. J., Paoli, G., Dodson, G. (1998) Annu. Rev. Biophys. Biomol. Struct. 27, 1-34.
    • (1998) , vol.27 , pp. 1-34
    • Perutz, M.1    Wilkinson, A.J.2    Paoli, G.3    Dodson, G.4
  • 59
    • 0001683176 scopus 로고
    • Allosteric inhibition of rat liver fructose 1,6-diphosphatase by adenosine 5'-monophosphate
    • Taketa, K., Pogell, B.N. (1965) Allosteric inhibition of rat liver fructose 1,6-diphosphatase by adenosine 5'-monophosphate, J. Biol. Chem. 240, 651-662.
    • (1965) J. Biol. Chem. , vol.240 , pp. 651-662
    • Taketa, K.1    Pogell, B.N.2
  • 61
    • 0000977357 scopus 로고
    • Allosteric linkage
    • Wyman, J. (1967) Allosteric linkage, J. Am. Chem. Soc. 89, 2202-2218.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 2202-2218
    • Wyman, J.1
  • 62
    • 0004244695 scopus 로고
    • Binding and Linkage
    • University Science Books, Mill Valley, CA
    • Wyman, J., Gill, S. J. (1990) Binding and Linkage, University Science Books, Mill Valley, CA.
    • (1990)
    • Wyman, J.1    Gill, S.J.2
  • 64
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • Briggs, G.E., Haldane, J.B.S. (1925) A note on the kinetics of enzyme action, Biochem. J. 19, 338-339.
    • (1925) Biochem. J. , vol.19 , pp. 338-339
    • Briggs, G.E.1    Haldane, J.B.S.2
  • 65
    • 0001284812 scopus 로고
    • Enzyme action
    • Brown, A.J. (1902) Enzyme action, J. Chem. Soc. 81, 373-388.
    • (1902) J. Chem. Soc. , vol.81 , pp. 373-388
    • Brown, A.J.1
  • 66
    • 0001705279 scopus 로고
    • Theorie generale de l'action de quelques diastases
    • Henri, V. (1902) Theorie generale de l'action de quelques diastases, C. R. Acad. Sci. 135, 916-919.
    • (1902) C. R. Acad. Sci. , vol.135 , pp. 916-919
    • Henri, V.1
  • 67
    • 0000870544 scopus 로고
    • Die Kinetik der Invertinwirkung
    • Michaelis, L., Menten, M.L. (1913) Die Kinetik der Invertinwirkung, Biochem. Z. 49, 333-369.
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 68
    • 0021012118 scopus 로고
    • Some recent advances in enzyme kinetics
    • Wharton, C.W. (1983) Some recent advances in enzyme kinetics, Biochem. Soc. Trans. 11, 817-825.
    • (1983) Biochem. Soc. Trans. , vol.11 , pp. 817-825
    • Wharton, C.W.1
  • 69
    • 0010731666 scopus 로고
    • Studies of the enzyme fumarase. VII Series solutions of integrated rate equations for irreversible and reversible Michaelis-Menten mechanism
    • Alberty, R.A., Koerber, B.M. (1957) Studies of the enzyme fumarase. VII Series solutions of integrated rate equations for irreversible and reversible Michaelis-Menten mechanism, J. Am. Chem. Soc. 79, 6379-6382.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 6379-6382
    • Alberty, R.A.1    Koerber, B.M.2
  • 70
    • 0014939384 scopus 로고
    • A method for the kinetic analysis of progress curves using horse serum cholin esterase as a model
    • Balcom, J.K., Fitch, W.M. (1945) A method for the kinetic analysis of progress curves using horse serum cholin esterase as a model, J. Biol. Chem. 245, 1637-1647.
    • (1945) J. Biol. Chem. , vol.245 , pp. 1637-1647
    • Balcom, J.K.1    Fitch, W.M.2
  • 71
    • 0020123472 scopus 로고
    • Initial rates. A new plot
    • Boeker, E.A. (1982) Initial rates. A new plot, Biochem. J. 203, 117-123.
    • (1982) Biochem. J. , vol.203 , pp. 117-123
    • Boeker, E.A.1
  • 72
    • 0016767575 scopus 로고
    • The use of the direct linear plot for determining initial velocities
    • Cornish-Bowden, A. (1975) The use of the direct linear plot for determining initial velocities, Biochem. J. 149, 305-312.
    • (1975) Biochem. J. , vol.149 , pp. 305-312
    • Cornish-Bowden, A.1
  • 73
    • 0017855795 scopus 로고
    • Estimation of Michaelis constant and maximum velocity from the direct linear plot
    • Cornish-Bowden, A., Eisenthal, R. (1978) Estimation of Michaelis constant and maximum velocity from the direct linear plot, Biochim. Biophys. Acta 523, 268-272.
    • (1978) Biochim. Biophys. Acta , vol.523 , pp. 268-272
    • Cornish-Bowden, A.1    Eisenthal, R.2
  • 74
    • 17144365959 scopus 로고
    • Graphical determination of equilibrium constants
    • Dixon, M. (1965) Graphical determination of equilibrium constants, Biochem. J. 94, 760-762.
    • (1965) Biochem. J. , vol.94 , pp. 760-762
    • Dixon, M.1
  • 75
    • 0002372921 scopus 로고
    • The inhibition of cholinesterase by physostigmine and prostigmine
    • Eadie, G.S. (1942) The inhibition of cholinesterase by physostigmine and prostigmine, J. Biol. Chem. 146, 85-93.
    • (1942) J. Biol. Chem. , vol.146 , pp. 85-93
    • Eadie, G.S.1
  • 76
    • 0016167076 scopus 로고
    • The direct linear plot. A new graphical procedure for estimating enzyme parameters
    • Eisenthal, R., Cornish-Bowden, A. (1974) The direct linear plot. A new graphical procedure for estimating enzyme parameters, Biochem. J. 139, 715-720.
    • (1974) Biochem. J. , vol.139 , pp. 715-720
    • Eisenthal, R.1    Cornish-Bowden, A.2
  • 77
    • 0342855486 scopus 로고
    • The evaluation of the kinetic constants of enzyme catalyzed reactions
    • Foster, R.J., Niemann, C. (1953) The evaluation of the kinetic constants of enzyme catalyzed reactions, Proc. Natl. Acad. Sci. USA 39, 999-1003.
    • (1953) Proc. Natl. Acad. Sci. USA , vol.39 , pp. 999-1003
    • Foster, R.J.1    Niemann, C.2
  • 78
    • 0003751143 scopus 로고
    • Allgemeine Chemie der Enzyme
    • Steinkopff, Dresden & Leipzig
    • Haldane, J.B.S., Stern, K.G. (1932) Allgemeine Chemie der Enzyme. Steinkopff, Dresden & Leipzig.
    • (1932)
    • Haldane, J.B.S.1    Stern, K.G.2
  • 79
    • 0001465376 scopus 로고
    • Studies on plant amylases. The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley
    • Hanes, C.S. (1932) Studies on plant amylases. The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley, Biochem. J. 26, 1406-1421.
    • (1932) Biochem. J. , vol.26 , pp. 1406-1421
    • Hanes, C.S.1
  • 80
    • 0007292157 scopus 로고
    • Specificity of esterases. Identification of two pancreatic aliesterases
    • Hofstee, B.H.J. (1952) Specificity of esterases. Identification of two pancreatic aliesterases, J. Biol. Chem. 199, 357-364.
    • (1952) J. Biol. Chem. , vol.199 , pp. 357-364
    • Hofstee, B.H.J.1
  • 81
    • 0003190286 scopus 로고
    • The evaluation of the kinetics of enzyme-catalzed reactions by procedures based upon integrated rate equation
    • Jennings, R.R., Niemann, C. (1954) The evaluation of the kinetics of enzyme-catalzed reactions by procedures based upon integrated rate equation, J. Am. Chem. Soc. 77, 5432-5433.
    • (1954) J. Am. Chem. Soc. , vol.77 , pp. 5432-5433
    • Jennings, R.R.1    Niemann, C.2
  • 82
    • 0013934919 scopus 로고
    • A modified graphical method for determination of equilibrium constants
    • Kilroe-Smith, J.A. (1966) A modified graphical method for determination of equilibrium constants, Biochem. J. 100, 334-335.
    • (1966) Biochem. J. , vol.100 , pp. 334-335
    • Kilroe-Smith, J.A.1
  • 83
    • 0015236546 scopus 로고
    • Enzymic parameters: Measurement of V and Km
    • Lee, H.J., Wilson, I.B. (1971) Enzymic parameters: Measurement of V and Km, Biochim. Biophys. Acta 242, 519-522.
    • (1971) Biochim. Biophys. Acta , vol.242 , pp. 519-522
    • Lee, H.J.1    Wilson, I.B.2
  • 84
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver, H., Burk, D. (1934) The determination of enzyme dissociation constants, J. Am. Chem. Soc. 56, 658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 85
    • 0016941453 scopus 로고
    • The analysis of kinetic data in biochemistry. A critical evaluation of methods
    • Markus, M., Hess, B., Ottaway, J.H., Cornish-Bowden, A. (1976) The analysis of kinetic data in biochemistry. A critical evaluation of methods, FEBS Lett. 63, 225-230.
    • (1976) FEBS Lett. , vol.63 , pp. 225-230
    • Markus, M.1    Hess, B.2    Ottaway, J.H.3    Cornish-Bowden, A.4
  • 86
    • 0017822768 scopus 로고
    • An evaluation of methods for determining initial velocities of enzyme-catalysed reactions from progress curves
    • Nimmo, I.A., Atkins, G.L. (1978) An evaluation of methods for determining initial velocities of enzyme-catalysed reactions from progress curves, Biochem. Soc. Trans. 6, 548-550.
    • (1978) Biochem. Soc. Trans. , vol.6 , pp. 548-550
    • Nimmo, I.A.1    Atkins, G.L.2
  • 87
    • 0018722047 scopus 로고
    • Kinetic analysis of progress curves
    • Orsi, B.A., Tipton, K.F. (1979) Kinetic analysis of progress curves, Methods Enzymol. 63, 159-183.
    • (1979) Methods Enzymol. , vol.63 , pp. 159-183
    • Orsi, B.A.1    Tipton, K.F.2
  • 88
    • 0018690805 scopus 로고
    • Plotting methods of enzyme rate data
    • Rudolph, F.B., Fromm, H.J. (1979) Plotting methods of enzyme rate data, Methods Enzymol. 63, 138-159.
    • (1979) Methods Enzymol. , vol.63 , pp. 138-159
    • Rudolph, F.B.1    Fromm, H.J.2
  • 89
    • 0014669596 scopus 로고
    • Use of integrated rate equations in estimating the kinetic constants of enzyme-catalyzed reactions
    • Schwert, G.W. (1969) Use of integrated rate equations in estimating the kinetic constants of enzyme-catalyzed reactions, J. Biol. Chem. 244, 1278-1284.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1278-1284
    • Schwert, G.W.1
  • 90
    • 0019540281 scopus 로고
    • An easy method for the determination of initial rates
    • Waley, S.G. (1981) An easy method for the determination of initial rates, Biochem. J.193, 1009-1012.
    • (1981) Biochem. J , vol.193 , pp. 1009-1012
    • Waley, S.G.1
  • 92
    • 0005499841 scopus 로고
    • Statistical estimations of enzyme kinetics
    • Wilkinson, G.N. (1961) Statistical estimations of enzyme kinetics, Biochem. J. 80, 324-332.
    • (1961) Biochem. J. , vol.80 , pp. 324-332
    • Wilkinson, G.N.1
  • 93
    • 77049143386 scopus 로고
    • The determination of the enzyme inhibition constants
    • Dixon, M. (1953) The determination of the enzyme inhibition constants, Biochem. J. 55, 170-171.
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 94
    • 0015378776 scopus 로고
    • The graphical determination of Km and Ki
    • Dixon, M. (1972) The graphical determination of Km and Ki, Biochem. J. 129, 197-202.
    • (1972) Biochem. J. , vol.129 , pp. 197-202
    • Dixon, M.1
  • 95
    • 0000591627 scopus 로고
    • Sulfonyl fluorides as inhibitors of esterases. I. Rates of reaction with aceylcholinesterase, chymotrypsin, and trypsin
    • Fahrney, D.E., Gold, A.M. (1963) Sulfonyl fluorides as inhibitors of esterases. I. Rates of reaction with aceylcholinesterase, chymotrypsin, and trypsin, J. Am. Chem. Soc. 85, 997-1000.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 997-1000
    • Fahrney, D.E.1    Gold, A.M.2
  • 96
    • 0017072736 scopus 로고
    • Transition state analogs for thiamin pyrophosphate-dependent enzymes
    • Gutowski, J.A., Lienhard, G.E. (1976) Transition state analogs for thiamin pyrophosphate-dependent enzymes, J. Biol. Chem. 251, 2863-2688.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2863-2688
    • Gutowski, J.A.1    Lienhard, G.E.2
  • 97
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R. & Wilson, I.B. (1962) Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase, J. Biol. Chem. 237, 3245-3249.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 98
    • 27944458409 scopus 로고    scopus 로고
    • Enzymatic transition states and transition state analogs
    • Schramm, V.L. (2005) Enzymatic transition states and transition state analogs, Curr. Opin. Struct. Biol. 15, 604-613.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 604-613
    • Schramm, V.L.1
  • 100
    • 0001061490 scopus 로고
    • The rate equation for an enzymatic reaction
    • 1st edn, Boyer, P.D., Lardy, H., Myrbäck, K. (Eds.), Academic Press, New York
    • Alberty, R.A. (1959) The rate equation for an enzymatic reaction. The Enzymes, 1st edn, Boyer, P.D., Lardy, H., Myrbäck, K. (Eds.), Academic Press, New York, Vol. 1, pp. 143-155.
    • (1959) The Enzymes , vol.1 , pp. 143-155
    • Alberty, R.A.1
  • 101
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations
    • Cleland, W.W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations, Biochim. Biophys. Acta 67, 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 102
    • 50549188738 scopus 로고    scopus 로고
    • II. Inhibition: Nomenclature and theory
    • II. Inhibition: Nomenclature and theory, Biochim. Biophys. Acta 67, 173-187.
    • Biochim. Biophys. Acta , vol.67 , pp. 173-187
  • 103
    • 50549155520 scopus 로고    scopus 로고
    • III. Prediction of initial velocity and inhibition patterns by inspection
    • III. Prediction of initial velocity and inhibition patterns by inspection, Biochim. Biophys. Acta 67, 188-196.
    • Biochim. Biophys. Acta , vol.67 , pp. 188-196
  • 104
    • 0001594119 scopus 로고
    • Initial steady-state velocities in the evaluation of enzyme-coenzyme-substrate reaction mechanism
    • Dalziel, K. (1957) Initial steady-state velocities in the evaluation of enzyme-coenzyme-substrate reaction mechanism, Acta Chem. Scand. 11, 1706-1723.
    • (1957) Acta Chem. Scand. , vol.11 , pp. 1706-1723
    • Dalziel, K.1
  • 105
    • 0014941719 scopus 로고
    • A simplified schematic method for deriving steady-state equations using a modification of the "Theory of Graphs" procedure
    • Fromm, H.J. (1970) A simplified schematic method for deriving steady-state equations using a modification of the "Theory of Graphs" procedure, Biochem. Biophys. Res. Commun. 40, 692-697.
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 692-697
    • Fromm, H.J.1
  • 106
    • 33947472850 scopus 로고
    • A schematic method for deriving the rate laws for enzyme-catalyzed reactions
    • King, E.L. & Altman, C. (1965) A schematic method for deriving the rate laws for enzyme-catalyzed reactions, J. Phys. Chem. 60, 1375-1378.
    • (1965) J. Phys. Chem. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 107
    • 0037487968 scopus 로고
    • A new method for solving the problems of the stationary kinetics of enzymological reactions
    • Volkenstein, M.V. & Goldstein, B.N. (1966) A new method for solving the problems of the stationary kinetics of enzymological reactions, Biochim. Biophys. Acta 115, 471-477.
    • (1966) Biochim. Biophys. Acta , vol.115 , pp. 471-477
    • Volkenstein, M.V.1    Goldstein, B.N.2
  • 108
    • 0000804930 scopus 로고
    • Über die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Säuren
    • Arrhenius, S. (1889) Über die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Säuren, Z. Phys. Chem. 4, 226-248.
    • (1889) Z. Phys. Chem. , vol.4 , pp. 226-248
    • Arrhenius, S.1
  • 109
    • 0004262303 scopus 로고
    • Enzymes
    • 3rd edn. Academic Press, New York
    • Dixon, M., Webb, E.C. (1979) Enzymes, 3rd edn. Academic Press, New York.
    • (1979)
    • Dixon, M.1    Webb, E.C.2
  • 110
    • 2142746284 scopus 로고
    • The activated complex in chemical reactions
    • Eyring, H. (1935) The activated complex in chemical reactions, J. Chem. Phys. 3, 107-115.
    • (1935) J. Chem. Phys. , vol.3 , pp. 107-115
    • Eyring, H.1
  • 111
    • 0018722048 scopus 로고
    • Temperature effects in enzyme kinetics
    • Laidler, K.J., Peterman, B.F. (1979) Temperature effects in enzyme kinetics, Methods Enzymol. 63, 234-257.
    • (1979) Methods Enzymol. , vol.63 , pp. 234-257
    • Laidler, K.J.1    Peterman, B.F.2
  • 113
    • 0021348394 scopus 로고
    • Cooperativity in highly aggregated systems
    • Bisswanger, H. (1984) Cooperativity in highly aggregated systems, J. Biol. Chem. 259, 2457-2465.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2457-2465
    • Bisswanger, H.1
  • 115
    • 0016150841 scopus 로고
    • Sigmoidal kinetics of monomeric ribonuclease I due to ligand-induced shifts of conformation equilibrium
    • Rübsamen, H., Khandker, R., Witzel, H. (1974) Sigmoidal kinetics of monomeric ribonuclease I due to ligand-induced shifts of conformation equilibrium. Hoppe-Seyler's Z. Physiol. Chem. 355, 687-708.
    • (1974) Hoppe-Seyler's Z. Physiol. Chem , vol.355 , pp. 687-708
    • Rübsamen, H.1    Khandker, R.2    Witzel, H.3
  • 116
    • 0032845061 scopus 로고    scopus 로고
    • Determining transition states from kinetic isotope effects
    • Berti, P.J. (1999) Determining transition states from kinetic isotope effects, Methods Enzymol. 308, 355-397.
    • (1999) Methods Enzymol. , vol.308 , pp. 355-397
    • Berti, P.J.1
  • 117
    • 0003486985 scopus 로고
    • Initial Rate Enzyme Kinetics
    • Springer-Verlag, Berlin
    • Fromm, H.J. (1975) Initial Rate Enzyme Kinetics, Springer-Verlag, Berlin.
    • (1975)
    • Fromm, H.J.1
  • 118
    • 0018681639 scopus 로고
    • Derivation of initial velocity and isotope exchange rate equations
    • Huang, C.Y. (1979) Derivation of initial velocity and isotope exchange rate equations, Methods Enzymol. 63, 54-84.
    • (1979) Methods Enzymol. , vol.63 , pp. 54-84
    • Huang, C.Y.1
  • 119
    • 0003408336 scopus 로고
    • Catalysis in Chemistry and Enzymology
    • McGraw-Hill, New York
    • Jencks, W.P. (1969) Catalysis in Chemistry and Enzymology, McGraw-Hill, New York, pp. 243-281.
    • (1969) , pp. 243-281
    • Jencks, W.P.1
  • 120
    • 0041129019 scopus 로고
    • Isotope exchange methods for elucidating enzymic catalysis
    • Purich, D.L., Allison, R.D. (1980) Isotope exchange methods for elucidating enzymic catalysis, Methods Enzymol. 64, 3-46.
    • (1980) Methods Enzymol. , vol.64 , pp. 3-46
    • Purich, D.L.1    Allison, R.D.2
  • 121
    • 0344350017 scopus 로고
    • Kinetic isotope effects in enzymic reactions
    • 3rd edn. Boyer, P. (Ed.), Academic Press, New York
    • Richards, J.H. (1970) Kinetic isotope effects in enzymic reactions, The Enzymes, 3rd edn. Boyer, P. (Ed.), Academic Press, New York, Vol. 2, pp. 321-333.
    • (1970) The Enzymes , vol.2 , pp. 321-333
    • Richards, J.H.1
  • 122
    • 0026651086 scopus 로고
    • Small catalytic RNAs
    • Symons, R.H. (1992) Small catalytic RNAs, Annu. Rev. Biochem. 61, 641-671.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 641-671
    • Symons, R.H.1
  • 123
    • 0000421250 scopus 로고    scopus 로고
    • Mechanisms of ribozyme-mediated RNA cleavage
    • Kuimelis, R.G., McLaughlin, L.W. (1998) Mechanisms of ribozyme-mediated RNA cleavage, Chem. Rev. 98, 1027-1044.
    • (1998) Chem. Rev. , vol.98 , pp. 1027-1044
    • Kuimelis, R.G.1    McLaughlin, L.W.2
  • 125
    • 34250132252 scopus 로고
    • The Michaelis-Menten equation in the case of linear homopolymer substrates with different degrees of polymerization
    • Chetkarov, M.L., Kolev, D.N. (1984) The Michaelis-Menten equation in the case of linear homopolymer substrates with different degrees of polymerization, Monatsh. Chem. 115, 1405-1412.
    • (1984) Monatsh. Chem. , vol.115 , pp. 1405-1412
    • Chetkarov, M.L.1    Kolev, D.N.2
  • 126
    • 0014943898 scopus 로고
    • Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exoenzymes
    • Hiromi, K. (1970) Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exoenzymes, Biochem. Biophys. Res. Commun. 40, 1-6.
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 1-6
    • Hiromi, K.1
  • 127
    • 0004144099 scopus 로고
    • Membrane transport
    • Neuberger, A., van Deenen, L.L.M. (Eds.), Elsevier, Amsterdam
    • Bonting, S.L. & de Pont, J.J.H.H.M. (1981) Membrane transport, in New Comprehensive Biochemistry, Vol. 2, Neuberger, A., van Deenen, L.L.M. (Eds.), Elsevier, Amsterdam.
    • (1981) New Comprehensive Biochemistry , vol.2
    • Bonting, S.L.1    De Pont, J.J.H.H.M.2
  • 128
    • 0004212990 scopus 로고    scopus 로고
    • Interfacial Enzyme Kinetics
    • John Wiley & Sons, Chichester
    • Berg, O.G., Jain, M.K. (2002) Interfacial Enzyme Kinetics, John Wiley & Sons, Chichester.
    • (2002)
    • Berg, O.G.1    Jain, M.K.2
  • 129
    • 0004106381 scopus 로고
    • Biological Transport
    • 2nd edn. W.A. Benjamin, Inc. Reading, MA
    • Christensen, H.N. (1975) Biological Transport, 2nd edn. W.A. Benjamin, Inc. Reading, MA.
    • (1975)
    • Christensen, H.N.1
  • 130
    • 0017268663 scopus 로고
    • Kinetic behavior of immobilized enzyme systems
    • Goldstein, L. (1976) Kinetic behavior of immobilized enzyme systems, Methods Enzymol. 44, 397-443.
    • (1976) Methods Enzymol. , vol.44 , pp. 397-443
    • Goldstein, L.1
  • 131
    • 0018814280 scopus 로고
    • The kinetics of immobilized enzyme systems
    • Laidler, K.J., Bunting, P.S. (1980) The kinetics of immobilized enzyme systems, Methods Enzymol. 61, 227-248.
    • (1980) Methods Enzymol. , vol.61 , pp. 227-248
    • Laidler, K.J.1    Bunting, P.S.2
  • 132
    • 2142780103 scopus 로고
    • Immobilized enzyme principles
    • in Applied Biochemistry and Bioengineering. Academic Press, New York
    • Wingard, L.B., Katchalski-Katzir, E., Goldstein, L. (1976) Immobilized enzyme principles, in Applied Biochemistry and Bioengineering. Academic Press, New York.
    • (1976)
    • Wingard, L.B.1    Katchalski-Katzir, E.2    Goldstein, L.3
  • 133
    • 0015739762 scopus 로고
    • Effect of internal diffusion in heterogeneous enzyme systems: Evaluation of true kinetic parameters and substrate diffusivity
    • Engasser, J.-M., Horvath, C. (1973) Effect of internal diffusion in heterogeneous enzyme systems: Evaluation of true kinetic parameters and substrate diffusivity, J. Theor. Biol. 42, 137-155.
    • (1973) J. Theor. Biol. , vol.42 , pp. 137-155
    • Engasser, J.-M.1    Horvath, C.2
  • 134
    • 23944518551 scopus 로고    scopus 로고
    • Allgemeine und spezielle Pharmakologie und Toxikologie
    • Aktories, K., Förstermann, U., Hofmann F., Starke, K. (2005) Allgemeine und spezielle Pharmakologie und Toxikologie, 9.
    • (2005) , pp. 9
    • Aktories, K.1    Förstermann, U.2    Hofmann, F.3    Starke, K.4
  • 135
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Aufl. Urban & Fischer, München, Jena. Cleland, W.W. (1979) Statistical analysis of enzyme kinetic data, Methods Enzymol. 63, 103-138.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Urban, A.1    Fischer, M.2    Cleland Jena, W.W.3
  • 136
    • 0004205267 scopus 로고    scopus 로고
    • Fundamentals of Enzyme Kinetics
    • Portland Press, London
    • Cornish-Bowden, A. (1995) Fundamentals of Enzyme Kinetics, Portland Press, London.
    • (1995)
    • Cornish-Bowden, A.1
  • 137
    • 0022499213 scopus 로고
    • Robust regression of enzyme kinetics
    • Cornish-Bowden, A., Endrenyi, L. (1986) Robust regression of enzyme kinetics, Biochem. J. 234, 21-29.
    • (1986) Biochem. J. , vol.234 , pp. 21-29
    • Cornish-Bowden, A.1    Endrenyi, L.2
  • 138
    • 0042752842 scopus 로고
    • Elementare Tests zur Beurteilung von Meßdaten
    • 2nd edn. Bibliographisches Institut, Mannheim
    • Kaiser, R.E., Mühlbauer, J.A. (1983) Elementare Tests zur Beurteilung von Meßdaten, 2nd edn. Bibliographisches Institut, Mannheim.
    • (1983)
    • Kaiser, R.E.1    Mühlbauer, J.A.2
  • 139
    • 78449307994 scopus 로고
    • Einführung in die Statistik
    • B.G. Teubner, Stuttgart
    • Lehn, J., Wegmann, H. (1985) Einführung in die Statistik, B.G. Teubner, Stuttgart.
    • (1985)
    • Lehn, J.1    Wegmann, H.2
  • 140
    • 0011094147 scopus 로고
    • Fehleranalyse
    • VCH, Weinheim
    • Taylor, J.R. (1988) Fehleranalyse, VCH, Weinheim.
    • (1988)
    • Taylor, J.R.1
  • 141
    • 0004232308 scopus 로고
    • Biostatistical Analysis
    • 2nd edn. Prentice-Hall Inc., Englewood Cliffs, New Jersey, USA
    • Zar, J.H. (1984) Biostatistical Analysis, 2nd edn. Prentice-Hall Inc., Englewood Cliffs, New Jersey, USA.
    • (1984)
    • Zar, J.H.1
  • 142
    • 0003443846 scopus 로고
    • Methods of Enzymatic Analysis
    • Verlag Chemie, Weinheim
    • Bergmeyer, H.U. (1983) Methods of Enzymatic Analysis, Verlag Chemie, Weinheim.
    • (1983)
    • Bergmeyer, H.U.1
  • 143
    • 0004273756 scopus 로고
    • Experimental Biochemistry
    • W.H. Freeman, San Francisco
    • Clark, J. M., Switzer, R.L. (1977) Experimental Biochemistry, W.H. Freeman, San Francisco.
    • (1977)
    • Clark, J.M.1    Switzer, R.L.2
  • 144
    • 0004268866 scopus 로고
    • Enzyme Assays. A Practical Approach
    • IRL Press, Oxford
    • Eisenthal, R., Danson, J. (1992) Enzyme Assays. A Practical Approach, IRL Press, Oxford.
    • (1992)
    • Eisenthal, R.1    Danson, J.2
  • 145
    • 0003731363 scopus 로고
    • Manometric and Biochemical Techniques
    • 5th edn. Burgess, Minneapolis
    • Umbreit, W.W., Burris, R. H., Stauffer, J.F. (1972) Manometric and Biochemical Techniques, 5th edn. Burgess, Minneapolis.
    • (1972)
    • Umbreit, W.W.1    Burris, R.H.2    Stauffer, J.F.3
  • 146
    • 0011062561 scopus 로고
    • Principles and Techniques of Practical Biochemistry
    • Edward Arnold, London
    • Williams, B. L., Wilson, K. (1975) Principles and Techniques of Practical Biochemistry, Edward Arnold, London.
    • (1975)
    • Williams, B.L.1    Wilson, K.2
  • 147
    • 0002624023 scopus 로고
    • Molecular sieve methods of analysis
    • in Neurath, H., Hill, R. L. (Eds.), 3rd edn, Academic Press, New York
    • Ackers, K. G. (1975) Molecular sieve methods of analysis, in Neurath, H., Hill, R. L. (Eds.) The Proteins, 3rd edn, Academic Press, New York, Vol. 1, pp. 1-94.
    • (1975) The Proteins , vol.1 , pp. 1-94
    • Ackers, K.G.1
  • 148
    • 0018756568 scopus 로고
    • Application of the miniature ultracentrifuge in receptor-binding assays
    • Alberts, R.W., Krishnan, N. (1979) Application of the miniature ultracentrifuge in receptor-binding assays, Anal. Biochem. 96, 396-402.
    • (1979) Anal. Biochem. , vol.96 , pp. 396-402
    • Alberts, R.W.1    Krishnan, N.2
  • 149
    • 0015082299 scopus 로고
    • Molecular sieve studies of interacting protein systems. Direct optical scanning method for ligand-macromolecule binding studies
    • Brumbaugh, E. E., Ackers, K.G. (1974) Molecular sieve studies of interacting protein systems. Direct optical scanning method for ligand-macromolecule binding studies, Anal. Biochem. 41, 543-559.
    • (1974) Anal. Biochem. , vol.41 , pp. 543-559
    • Brumbaugh, E.E.1    Ackers, K.G.2
  • 150
    • 67651132219 scopus 로고
    • Studies on the calcium-protein relationship with the aid of the ultracentrifuge
    • Chanutin, A., Ludewig, S., Masket, A.V. (1942) Studies on the calcium-protein relationship with the aid of the ultracentrifuge, J. Biol. Chem. 143, 737-751.
    • (1942) J. Biol. Chem. , vol.143 , pp. 737-751
    • Chanutin, A.1    Ludewig, S.2    Masket, A.V.3
  • 151
    • 0014690150 scopus 로고
    • Binding of diffusible molecules by macromolecules: Rapid measurements by rate of dialysis
    • Colowick, S. P., Womack, F. C. (1969) Binding of diffusible molecules by macromolecules: Rapid measurements by rate of dialysis, J. Biol. Chem. 244, 774-777.
    • (1969) J. Biol. Chem. , vol.244 , pp. 774-777
    • Colowick, S.P.1    Womack, F.C.2
  • 152
    • 0018782944 scopus 로고
    • Measurement of macromolecule binding constants by a sucrose gradient band
    • Draper, D. E., Hippel, P.H. (1979) Measurement of macromolecule binding constants by a sucrose gradient band, Biochemistry 18, 753-760.
    • (1979) Biochemistry , vol.18 , pp. 753-760
    • Draper, D.E.1    Hippel, P.H.2
  • 153
    • 0014670222 scopus 로고
    • Enzymatic synthesis of deoxyribonucleic acid. Binding of triphosphates to deoxyribonucleic acid polymerase
    • Englund, P. E., Huberman, J. A., Jovin, T. M., Kornberg, A. (1969) Enzymatic synthesis of deoxyribonucleic acid. Binding of triphosphates to deoxyribonucleic acid polymerase, J. Biol. Chem. 244, 3038-3044.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3038-3044
    • Englund, P.E.1    Huberman, J.A.2    Jovin, T.M.3    Kornberg, A.4
  • 154
    • 50549168907 scopus 로고
    • Measuring of protein-binding by gel filtration
    • Hummel, J. P., Dreyer, W. J. (1962) Measuring of protein-binding by gel filtration, Biochim. Biophys. Acta 63, 530-532.
    • (1962) Biochim. Biophys. Acta , vol.63 , pp. 530-532
    • Hummel, J.P.1    Dreyer, W.J.2
  • 155
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behavior of enzymes. Application of protein mixtures
    • Martin, R. G., Ames, B.N. (1961) A method for determining the sedimentation behavior of enzymes. Application of protein mixtures, J. Biol. Chem. 236, 1372-1379.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 156
    • 25744461229 scopus 로고
    • The interaction of ribonuclease with purine and pyrimidine phosphates. Binding of adenosine-5'-monophosphate to ribonuclease
    • Myer, Y.P. & Schellman, J. A. (1962) The interaction of ribonuclease with purine and pyrimidine phosphates. Binding of adenosine-5'-monophosphate to ribonuclease, Biochim. Biophys. Acta 55, 361-373.
    • (1962) Biochim. Biophys. Acta , vol.55 , pp. 361-373
    • Myer, Y.P.1    Schellman, J.A.2
  • 157
    • 0014679216 scopus 로고
    • A rapid and sensitive method for measuring the binding of radioactive ligands to proteins
    • Paulus, H. (1969) A rapid and sensitive method for measuring the binding of radioactive ligands to proteins, Anal. Biochem. 32, 91-100.
    • (1969) Anal. Biochem. , vol.32 , pp. 91-100
    • Paulus, H.1
  • 158
    • 0000611841 scopus 로고
    • Ultracentrifugation studies with absorption optics. Analysis of interacting systems involving macromolecules and small molecules
    • Steinberg, I. Z., Schachman, H.K. (1966) Ultracentrifugation studies with absorption optics. Analysis of interacting systems involving macromolecules and small molecules, Biochemistry 5, 3728-3747.
    • (1966) Biochemistry , vol.5 , pp. 3728-3747
    • Steinberg, I.Z.1    Schachman, H.K.2
  • 159
    • 0017178743 scopus 로고
    • Determination of ligand binding: Partial and full saturation of aspartate transcarbamylase. Applicability of a filter assay to weakly binding ligands
    • Suter, P., Rosenbusch, J. (1976) Determination of ligand binding: Partial and full saturation of aspartate transcarbamylase. Applicability of a filter assay to weakly binding ligands, J. Biol. Chem. 251, 5986-5991.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5986-5991
    • Suter, P.1    Rosenbusch, J.2
  • 160
    • 0016264034 scopus 로고
    • On the specificity of the binding of estradiol receptor protein to deoxyribonucleic acid
    • Yamamoto, K. R., Alberts, B. (1974) On the specificity of the binding of estradiol receptor protein to deoxyribonucleic acid, J. Biol. Chem. 249, 7076-7086.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7076-7086
    • Yamamoto, K.R.1    Alberts, B.2
  • 161
    • 0037088751 scopus 로고    scopus 로고
    • Analyzing biomolecular interactions
    • Wilson, W. D. (2002) Analyzing biomolecular interactions, Science 295, 2103-2105.
    • (2002) Science , vol.295 , pp. 2103-2105
    • Wilson, W.D.1
  • 162
    • 0026551323 scopus 로고
    • Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis
    • Fägerstam, L. G., Frostell-Karlsson, A., Karlsson, R., Persson, B., Rönnberg, I. (1992) Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis, J. Chromatogr. 597, 397-410.
    • (1992) J. Chromatogr. , vol.597 , pp. 397-410
    • Fägerstam, L.G.1    Frostell-Karlsson, A.2    Karlsson, R.3    Persson, B.4    Rönnberg, I.5
  • 164
    • 0001322362 scopus 로고
    • Continuous recording of blood oxygen tensions by polarography
    • Clark, L. C. Jr, Wolf, R., Granger, D., Taylor, Z. (1953) Continuous recording of blood oxygen tensions by polarography, J. Appl. Physiol. 6, 189-193.
    • (1953) J. Appl. Physiol. , vol.6 , pp. 189-193
    • Clark Jr, L.C.1    Wolf, R.2    Granger, D.3    Taylor, Z.4
  • 165
    • 0018853840 scopus 로고
    • Polarographic measurements of steady-state kinetics of oxygen uptake by biochemical samples
    • Degn, H., Lundsgaard, J. S., Peterson, L. C., Ormick, A. (1980) Polarographic measurements of steady-state kinetics of oxygen uptake by biochemical samples, Methods Biochem. Anal. 26, 47-77.
    • (1980) Methods Biochem. Anal. , vol.26 , pp. 47-77
    • Degn, H.1    Lundsgaard, J.S.2    Peterson, L.C.3    Ormick, A.4
  • 166
    • 0020024002 scopus 로고
    • Adaptation to polarographic oxygen sensors for biochemical assays
    • Lessler, M.A. (1982) Adaptation to polarographic oxygen sensors for biochemical assays, Methods Biochem. Anal. 28, 175-199.
    • (1982) Methods Biochem. Anal. , vol.28 , pp. 175-199
    • Lessler, M.A.1
  • 167
    • 0014437302 scopus 로고
    • Oxygen electrode measurements in biochemical analysis
    • Lessler, M. A., Bierley, G.P. (1969) Oxygen electrode measurements in biochemical analysis. Methods Biochem. Anal. 17, 1-29.
    • (1969) Methods Biochem. Anal , vol.17 , pp. 1-29
    • Lessler, M.A.1    Bierley, G.P.2
  • 168
    • 77956802513 scopus 로고
    • Electrode measurements of carbon dioxide
    • Nicolls, D.G., Garland, P. B. (1972) Electrode measurements of carbon dioxide, Methods Microbiol. 6B, 55-63.
    • (1972) Methods Microbiol , vol.6 B , pp. 55-63
    • Nicolls, D.G.1    Garland, P.B.2
  • 169
    • 0042665403 scopus 로고
    • Polarographic assay for malate synthase and citrate synthase
    • Weitzman, P. D. J. (1969) Polarographic assay for malate synthase and citrate synthase, Methods Enzymol. 13, 365-368.
    • (1969) Methods Enzymol. , vol.13 , pp. 365-368
    • Weitzman, P.D.J.1
  • 170
    • 0025285535 scopus 로고
    • Calorimetrically determined dynamics of complex unfolding transitions in proteins
    • Freire, E., van Ospold, W.W. (1990) Calorimetrically determined dynamics of complex unfolding transitions in proteins, Annu. Rev. Biophys. Biophys. Chem. 19, 159-188.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 159-188
    • Freire, E.1    Van Ospold, W.W.2
  • 171
    • 0004234796 scopus 로고
    • Grundlagen der Kalorimetrie
    • Verlag Chemie, Weinheim
    • Hemminger, W., Höhne, G. (1979) Grundlagen der Kalorimetrie, Verlag Chemie, Weinheim.
    • (1979)
    • Hemminger, W.1    Höhne, G.2
  • 172
    • 0019347063 scopus 로고
    • Thermodynamic flow methods in biochemistry, calorimetry, densitometry and dilatometry
    • Jolicoeur, C. (1981) Thermodynamic flow methods in biochemistry, calorimetry, densitometry and dilatometry, Methods Biochem. Anal. 21, 171-287.
    • (1981) Methods Biochem. Anal. , vol.21 , pp. 171-287
    • Jolicoeur, C.1
  • 173
    • 0017224208 scopus 로고
    • Calorimetry as an analytical tool in biochemistry and biology
    • Spink, C., Wadsö, I. (1976) Calorimetry as an analytical tool in biochemistry and biology, Methods Biochem. Anal. 23, 1-159.
    • (1976) Methods Biochem. Anal. , vol.23 , pp. 1-159
    • Spink, C.1    Wadsö, I.2
  • 174
    • 0025285535 scopus 로고
    • Calorimetrically determined dynamics of complex unfolding transitions in proteins
    • Freire, E., van Ospold, W.W. (1990) Calorimetrically determined dynamics of complex unfolding transitions in proteins, Annu. Rev. Biophys. Biophys. Chem. 19, 159-188.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 159-188
    • Freire, E.1    Van Ospold, W.W.2
  • 175
    • 0004234796 scopus 로고
    • Grundlagen der Kalorimetrie
    • Verlag Chemie, Weinheim
    • Hemminger, W., Höhne, G. (1979) Grundlagen der Kalorimetrie, Verlag Chemie, Weinheim.
    • (1979)
    • Hemminger, W.1    Höhne, G.2
  • 176
    • 0019347063 scopus 로고
    • Thermodynamic flow methods in biochemistry, calorimetry, densitometry and dilatometry
    • Jolicoeur, C. (1981) Thermodynamic flow methods in biochemistry, calorimetry, densitometry and dilatometry, Methods Biochem. Anal. 21, 171-287.
    • (1981) Methods Biochem. Anal. , vol.21 , pp. 171-287
    • Jolicoeur, C.1
  • 177
    • 0017224208 scopus 로고
    • Calorimetry as an analytical tool in biochemistry and biology
    • Spink, C., Wadsö, I. (1976) Calorimetry as an analytical tool in biochemistry and biology, Methods Biochem. Anal. 23, 1-159.
    • (1976) Methods Biochem. Anal. , vol.23 , pp. 1-159
    • Spink, C.1    Wadsö, I.2
  • 178
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotation dispersion of proteins and polypeptides
    • Adler, A. J., Greenfield, N.J., Fassman, G.D. (1973) Circular dichroism and optical rotation dispersion of proteins and polypeptides, Methods Enzymol. 27, 675-735.
    • (1973) Methods Enzymol. , vol.27 , pp. 675-735
    • Adler, A.J.1    Greenfield, N.J.2    Fassman, G.D.3
  • 179
    • 0001121643 scopus 로고
    • Fluorescence measurements
    • Brand, L., Witholt, B. (1961) Fluorescence measurements, Methods Enzymol. 11, 776-856.
    • (1961) Methods Enzymol. , vol.11 , pp. 776-856
    • Brand, L.1    Witholt, B.2
  • 180
    • 0015490257 scopus 로고
    • Fluorescence probes for structure
    • Brand, L., Gohlke, J. R. (1972) Fluorescence probes for structure, Annu. Rev. Biochem. 41, 843-868.
    • (1972) Annu. Rev. Biochem. , vol.41 , pp. 843-868
    • Brand, L.1    Gohlke, J.R.2
  • 181
    • 0000123572 scopus 로고
    • Photochemical action spectra of carbon monoxide-inhibited respiration
    • Castor, L. N., Chance, B. (1955) Photochemical action spectra of carbon monoxide-inhibited respiration, J. Biol. Chem. 217, 453-465.
    • (1955) J. Biol. Chem. , vol.217 , pp. 453-465
    • Castor, L.N.1    Chance, B.2
  • 183
    • 0003768043 scopus 로고
    • Biophysical and Biochemical Aspects of Fluorescence Spectroscopy
    • Plenum Press, New York
    • Dewey, T.G. (1991) Biophysical and Biochemical Aspects of Fluorescence Spectroscopy, Plenum Press, New York.
    • (1991)
    • Dewey, T.G.1
  • 184
    • 0015777319 scopus 로고
    • Ultraviolet difference spectroscopy-New techniques and applications
    • Donovan, J.W. (1973) Ultraviolet difference spectroscopy-New techniques and applications, Methods Enzymol. 27, 497-525.
    • (1973) Methods Enzymol. , vol.27 , pp. 497-525
    • Donovan, J.W.1
  • 185
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Eftink, M.R. (1989) Fluorescence techniques for studying protein structure, Methods Biochem. Anal. 35, 127-205.
    • (1989) Methods Biochem. Anal. , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 186
    • 0003920544 scopus 로고
    • Practical Handbook of Biochemistry and Molecular Biology
    • CRC Press, Boca Raton
    • Fasman, G. D. (1989) Practical Handbook of Biochemistry and Molecular Biology, CRC Press, Boca Raton.
    • (1989)
    • Fasman, G.D.1
  • 187
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • 6th Series
    • Förster, T. (1948) Zwischenmolekulare Energiewanderung und Fluoreszenz, Ann. Phys. 437, 6th Series, Vol. 2, pp. 55-75.
    • (1948) Ann. Phys , vol.437 , pp. 55-75
    • Förster, T.1
  • 188
    • 0003651759 scopus 로고
    • Spektroskopische Methoden in der Biochemie
    • Thieme, Stuttgart
    • Galla, H.-J. (1988) Spektroskopische Methoden in der Biochemie, Thieme, Stuttgart.
    • (1988)
    • Galla, H.-J.1
  • 189
    • 84889305071 scopus 로고
    • Struktur-Funktionsbeziehung im Pyruvatdehydrogenase-Multienzymkomplex aus Escherichia coli
    • Ph.D. Thesis, University of Tübingen, Germany
    • Graupe, K. (1982) Struktur-Funktionsbeziehung im Pyruvatdehydrogenase-Multienzymkomplex aus Escherichia coli, Ph.D. Thesis, University of Tübingen, Germany.
    • (1982)
    • Graupe, K.1
  • 190
    • 0020068544 scopus 로고
    • Reassociation of the pyruvate dehydrogenase complex from Escherichia coli: Kinetic measurements and binding studies by resonance energy transfer
    • Graupe, K., Abusaud, M., Karfunkel, H., Bisswanger, H. (1982) Reassociation of the pyruvate dehydrogenase complex from Escherichia coli: Kinetic measurements and binding studies by resonance energy transfer, Biochemistry 21, 1386-1394.
    • (1982) Biochemistry , vol.21 , pp. 1386-1394
    • Graupe, K.1    Abusaud, M.2    Karfunkel, H.3    Bisswanger, H.4
  • 191
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N.J., Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.J.1    Fasman, G.D.2
  • 192
    • 0003882533 scopus 로고
    • Practical Fluorescence
    • Marcel Dekker, New York
    • Guibault, G. G. (1990) Practical Fluorescence, Marcel Dekker, New York.
    • (1990)
    • Guibault, G.G.1
  • 193
    • 0038197047 scopus 로고    scopus 로고
    • IR Spektroscopy
    • Wiley-VCH, Weinheim
    • Günzler, H., Gremlich, H.-U. (2002) IR Spektroscopy, Wiley-VCH, Weinheim.
    • (2002)
    • Günzler, H.1    Gremlich, H.-U.2
  • 194
    • 0003272546 scopus 로고
    • Spectrophotometry and Spectrofluorimetry
    • IRL Press, Oxford
    • Harris, D.A., Bashford, C. L. (1987) Spectrophotometry and Spectrofluorimetry, IRL Press, Oxford.
    • (1987)
    • Harris, D.A.1    Bashford, C.L.2
  • 195
    • 0003490276 scopus 로고    scopus 로고
    • Handbook of Fluorescent Probes and Research Products
    • 9th edn. Molecular Probes, Eugene, Oregon
    • Haugland, R. P. (2002) Handbook of Fluorescent Probes and Research Products, 9th edn. Molecular Probes, Eugene, Oregon.
    • (2002)
    • Haugland, R.P.1
  • 196
    • 0000405849 scopus 로고
    • Difference spectroscopy
    • Herskovits, T.T. (1967) Difference spectroscopy, Methods Enzymol. 11, 748-775.
    • (1967) Methods Enzymol. , vol.11 , pp. 748-775
    • Herskovits, T.T.1
  • 197
    • 0021944965 scopus 로고
    • Circular dichroism and its empirical application to biopolymers
    • Johnson, W. C. (1985) Circular dichroism and its empirical application to biopolymers, Methods Biochem. Anal. 31, 61-163.
    • (1985) Methods Biochem. Anal. , vol.31 , pp. 61-163
    • Johnson, W.C.1
  • 198
    • 0004324750 scopus 로고    scopus 로고
    • Principles of Fluorescence Spectrocopy
    • 2nd edn, Kluwer Academic/Plenum Publisher, New York
    • Lakowicz, J. R. (1999) Principles of Fluorescence Spectrocopy, 2nd edn, Kluwer Academic/Plenum Publisher, New York.
    • (1999)
    • Lakowicz, J.R.1
  • 199
    • 0020674385 scopus 로고
    • Photochemical action spectra of CO-liganded terminal oxi dases using a liquid dye laser
    • Lloyd, D., Scott, R. I. (1983) Photochemical action spectra of CO-liganded terminal oxi dases using a liquid dye laser, Anal. Biochem. 128, 21-24.
    • (1983) Anal. Biochem. , vol.128 , pp. 21-24
    • Lloyd, D.1    Scott, R.I.2
  • 200
    • 85022557096 scopus 로고
    • Application of infrared and Raman spectroscopy to studies of protein conformation
    • in Kornberg, H.L. (ed.), Elsevier/North Holland, County Clare
    • Mendelsohn, R. (1978) Application of infrared and Raman spectroscopy to studies of protein conformation, in Kornberg, H.L. (ed.) Techniques in Protein and Enzyme Biochemistry. B109, pp. 1-28. Elsevier/North Holland, County Clare.
    • (1978) Techniques in Protein and Enzyme Biochemistry , vol.B109 , pp. 1-28
    • Mendelsohn, R.1
  • 201
    • 0001301977 scopus 로고
    • Polarisation de la Lumire de Fluorescence. Vie Moyenne des Molecules dans l'Etat excit
    • Perrin, F. (1926) Polarisation de la Lumire de Fluorescence. Vie Moyenne des Molecules dans l'Etat excit, J. Phys., Ser. VI 7, 390-401.
    • (1926) J. Phys., Ser. VI , vol.7 , pp. 390-401
    • Perrin, F.1
  • 202
    • 73049144001 scopus 로고
    • Far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on configuration
    • Rosenheck, K., Doty, P. (1961) Far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on configuration, Proc. Natl. Acad. Sci. USA 47, 1775-1785.
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1775-1785
    • Rosenheck, K.1    Doty, P.2
  • 203
    • 0017219061 scopus 로고
    • Recent advances in bioluminescence and chemoluminescence assay
    • Seitz, W. R., Neary, M.P. (1969) Recent advances in bioluminescence and chemoluminescence assay, Methods Biochem. Anal. 23, 161-188.
    • (1969) Methods Biochem. Anal. , vol.23 , pp. 161-188
    • Seitz, W.R.1    Neary, M.P.2
  • 204
    • 0008070897 scopus 로고
    • Sci. Pop. Coll. Gen. Educ. Univ. Tokyo
    • Shikari, M. (1969) Sci. Pop. Coll. Gen. Educ. Univ. Tokyo 19, 151.
    • (1969) , vol.19 , pp. 151
    • Shikari, M.1
  • 205
    • 0014229883 scopus 로고
    • Bioluminescence assay: Principles and practice
    • Strehler, B.L. (1968) Bioluminescence assay: Principles and practice, Methods Biochem. Anal. 16, 99-179.
    • (1968) Methods Biochem. Anal. , vol.16 , pp. 99-179
    • Strehler, B.L.1
  • 206
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer, L. (1968) Fluorescence spectroscopy of proteins, Science 162, 526-533.
    • (1968) Science , vol.162 , pp. 526-533
    • Stryer, L.1
  • 207
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer, L. (1978) Fluorescence energy transfer as a spectroscopic ruler, Annu. Rev. Biochem. 47, 819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 208
    • 77956794262 scopus 로고
    • Absorption, circular dichroism and optical rotary dispersion of polypeptides, proteins, prosthetic groups and biomembranes
    • in Neuberger, A., Van Deenen, L. L.M. (eds.), New Comprehensive Biochemistry 11A, Elsevier, Amsterdam
    • Urry, D.W. (1985) Absorption, circular dichroism and optical rotary dispersion of polypeptides, proteins, prosthetic groups and biomembranes, in Neuberger, A., Van Deenen, L. L.M. (eds.) Modern Physical Methods in Biochemistry, New Comprehensive Biochemistry 11A, Elsevier, Amsterdam, pp. 275-346.
    • (1985) Modern Physical Methods in Biochemistry , pp. 275-346
    • Urry, D.W.1
  • 209
    • 0003718955 scopus 로고    scopus 로고
    • Molecular Fluorescence
    • Principles and Applications, Wiley-VCH, Weinheim
    • Valeur, B. (2002) Molecular Fluorescence, Principles and Applications, Wiley-VCH, Weinheim.
    • (2002)
    • Valeur, B.1
  • 210
    • 0003605587 scopus 로고
    • Physical Biochemistry
    • Prentice Hall, Englewood Cliffs
    • Van Holde, K. E. (1985) Physical Biochemistry, Prentice Hall, Englewood Cliffs.
    • (1985)
    • Van Holde, K.E.1
  • 211
    • 0006518524 scopus 로고
    • Über das Absorptionsspektrum des Atmungsferments
    • Warburg, O. & Negelein, E. (1929) Über das Absorptionsspektrum des Atmungsferments, Biochem. Z. 214, 64-100.
    • (1929) Biochem. Z. , vol.214 , pp. 64-100
    • Warburg, O.1    Negelein, E.2
  • 212
    • 77956741418 scopus 로고
    • Ultraviolet spectra of proteins and amino acids
    • Wettlaufer, D.B. (1962) Ultraviolet spectra of proteins and amino acids, Adv. Protein Chem. 17, 303-390.
    • (1962) Adv. Protein Chem. , vol.17 , pp. 303-390
    • Wettlaufer, D.B.1
  • 213
    • 0022547914 scopus 로고
    • Infra-red and Raman spectroscopic studies of enzyme structure and function
    • Wharton, C.W. (1986) Infra-red and Raman spectroscopic studies of enzyme structure and function, Biochem. J. 233, 25-36.
    • (1986) Biochem. J. , vol.233 , pp. 25-36
    • Wharton, C.W.1
  • 214
    • 0016365689 scopus 로고
    • Stoppedflow circular dichroism: A fast-kinetic system
    • Bayley, P. M., Anson, M. (1975) Stoppedflow circular dichroism: A fast-kinetic system, Biopolymers 13, 401-405.
    • (1975) Biopolymers , vol.13 , pp. 401-405
    • Bayley, P.M.1    Anson, M.2
  • 215
    • 0013843361 scopus 로고
    • The kinetics of the trypsin-catalyzed hydrolysis of p-nitrophenyl-α-N-benzyloxycarbonyl-L-lysinate hydrochloride
    • Bender, M. L., Kzdy, F. J., Feder, J. (1965) The kinetics of the trypsin-catalyzed hydrolysis of p-nitrophenyl-α-N-benzyloxycarbonyl-L-lysinate hydrochloride, J. Am. Chem. Soc. 87, 4953-4954.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 4953-4954
    • Bender, M.L.1    Kzdy, F.J.2    Feder, J.3
  • 216
    • 0004202565 scopus 로고
    • Relaxation Kinetics. Academic Press
    • New York
    • Bernasconi, C.F. (1976) Relaxation Kinetics. Academic Press, New York.
    • (1976)
    • Bernasconi, C.F.1
  • 217
    • 0001208501 scopus 로고
    • Sudden freezing as a technique for the study of rapid reactions
    • Bray, R.C. (1961) Sudden freezing as a technique for the study of rapid reactions, Biochem. J. 81, 189-193.
    • (1961) Biochem. J. , vol.81 , pp. 189-193
    • Bray, R.C.1
  • 218
  • 219
    • 0004159907 scopus 로고
    • Rapid Mixing and Sampling Techniques in Biochemistry
    • Academic Press, New York
    • Chance, B., Eisenhardt, R. M., Gibson, Q.H., Lonberg-Holm, K. K. (1964) Rapid Mixing and Sampling Techniques in Biochemistry, Academic Press, New York.
    • (1964)
    • Chance, B.1    Eisenhardt, R.M.2    Gibson, Q.H.3    Lonberg-Holm, K.K.4
  • 220
    • 84882393844 scopus 로고
    • Rapid-Flow-Methods
    • in Weissberger, A. (ed.), J. Wiley & Sons, New York
    • Chance, B. (1974) Rapid-Flow-Methods, in Weissberger, A. (ed.) Techniques of Chemistry, Vol. VI, Part II, pp. 5-62. J. Wiley & Sons, New York.
    • (1974) Techniques of Chemistry , vol.VI , Issue.PART II , pp. 5-62
    • Chance, B.1
  • 221
    • 84889432578 scopus 로고
    • Pulse radiolyse
    • in Weissberger, A. (ed.), J. Wiley & Sons, New York
    • Dorfman, L.M. (1974) Pulse radiolyse, in Weissberger, A. (ed.) Techniques of Chemistry, Vol. VI, Part II, pp. 363-419. J. Wiley & Sons, New York.
    • (1974) Techniques of Chemistry , vol.VI , Issue.PART II , pp. 363-419
    • Dorfman, L.M.1
  • 222
    • 0343050678 scopus 로고
    • Theoretical basis of relaxation spectroscopy
    • in Weissberger, A. (ed.), J. Wiley & Sons, New York
    • Eigen, M., De Mayer, L. (1974) Theoretical basis of relaxation spectroscopy, in Weissberger, A. (ed.) Techniques of Chemistry, Vol. VI, Part II, pp. 63-146. J. Wiley & Sons, New York.
    • (1974) Techniques of Chemistry , vol.VI , Issue.PART II , pp. 63-146
    • Eigen, M.1    De Mayer, L.2
  • 223
    • 0000125188 scopus 로고
    • Relaxation methods
    • in Friess, S. L., Lewis, E. S., Weissberger, A. (eds.), John Wiley & Sons, New York
    • Eigen, M., De Mayer, L. (1963) Relaxation methods, in Friess, S. L., Lewis, E. S., Weissberger, A. (eds.) Techniques of Organic Chemistry, Vol. VIII, Part II, pp. 895-1054. John Wiley & Sons, New York.
    • (1963) Techniques of Organic Chemistry , vol.VIII , Issue.PART II , pp. 895-1054
    • Eigen, M.1    De Mayer, L.2
  • 224
    • 0344901806 scopus 로고
    • Versatile stopped-flow temperature jump apparatus
    • Erman, J. E., Hammes, G. G. (1966) Versatile stopped-flow temperature jump apparatus, Rev. Sci. Instrum. 37, 746-750.
    • (1966) Rev. Sci. Instrum. , vol.37 , pp. 746-750
    • Erman, J.E.1    Hammes, G.G.2
  • 225
    • 0016737868 scopus 로고
    • Demonstration of two reaction pathways for the amino acylation of tRNA. Application of the pulsed quenched flow technique
    • Fersht, A. R., Jakes, R. (1975) Demonstration of two reaction pathways for the amino acylation of tRNA. Application of the pulsed quenched flow technique, Biochemistry 14, 3350-3356.
    • (1975) Biochemistry , vol.14 , pp. 3350-3356
    • Fersht, A.R.1    Jakes, R.2
  • 226
    • 0017716891 scopus 로고
    • Kinetics of the alkaline tetramer-dimer dissociation in liganded human hemoglobin: A laser light scattering stopped-flow study
    • Flamig, D.P., Parkhurst, L. J. (1977) Kinetics of the alkaline tetramer-dimer dissociation in liganded human hemoglobin: A laser light scattering stopped-flow study, Proc. Natl. Acad. Sci. USA 74, 3814-3816.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3814-3816
    • Flamig, D.P.1    Parkhurst, L.J.2
  • 227
    • 0000750623 scopus 로고
    • Apparatus for rapid and sensitive photometry
    • Gibson, Q.H., Milnes, L. (1964) Apparatus for rapid and sensitive photometry, Biochem. J. 91, 161-171.
    • (1964) Biochem. J. , vol.91 , pp. 161-171
    • Gibson, Q.H.1    Milnes, L.2
  • 228
    • 0016613648 scopus 로고
    • Concanavalin A: A stopped-flow nuclear magnetic resonance study of conformational changes induced by Mn++, Ca++, and α-methyl-D-mannoside
    • Grimaldi, J. J., Sykes, B. D. (1975) Concanavalin A: A stopped-flow nuclear magnetic resonance study of conformational changes induced by Mn++, Ca++, and α-methyl-D-mannoside, J. Biol. Chem. 250, 1618-1624.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1618-1624
    • Grimaldi, J.J.1    Sykes, B.D.2
  • 229
    • 0001564815 scopus 로고
    • Rapid mixing: Continuous flow
    • Gutfreund, H. (1969) Rapid mixing: Continuous flow, Methods Enzymol. 16, 229-249.
    • (1969) Methods Enzymol. , vol.16 , pp. 229-249
    • Gutfreund, H.1
  • 230
    • 0242503695 scopus 로고
    • The velocity with which carbon monoxide displaces oxygen from combination with haemoglobin
    • Hartridge, H., Roughton, F. J.W. (1923) The velocity with which carbon monoxide displaces oxygen from combination with haemoglobin, Proc. R. Soc. London, Ser. B 94, 336-367.
    • (1923) Proc. R. Soc. London, Ser. B , vol.94 , pp. 336-367
    • Hartridge, H.1    Roughton, F.J.W.2
  • 231
    • 0021096701 scopus 로고
    • Biological applications of picosecond spectroscopy
    • Hilinski, E. F., Rentzepis, P.M. (1983) Biological applications of picosecond spectroscopy, Nature 302, 481-487.
    • (1983) Nature , vol.302 , pp. 481-487
    • Hilinski, E.F.1    Rentzepis, P.M.2
  • 232
    • 0003565404 scopus 로고
    • Kinetics of Fast Enzyme Reactions
    • J. Wiley & Sons, New York
    • Hiromi, K. (1979) Kinetics of Fast Enzyme Reactions, J. Wiley & Sons, New York.
    • (1979)
    • Hiromi, K.1
  • 233
    • 0015159414 scopus 로고
    • A nanosecond temperature-jump apparatus
    • Hoffmann, G.W. (1971) A nanosecond temperature-jump apparatus, Rev. Sci. Instrum. 42, 1643-1647.
    • (1971) Rev. Sci. Instrum. , vol.42 , pp. 1643-1647
    • Hoffmann, G.W.1
  • 234
    • 36849104119 scopus 로고
    • Laser temperature-jump apparatus for relaxation studies in electrolytic solutions
    • Hoffmann, H., Yeager, E., Stuehr, J. (1968) Laser temperature-jump apparatus for relaxation studies in electrolytic solutions, Rev. Sci. Instrum. 39, 649-653.
    • (1968) Rev. Sci. Instrum. , vol.39 , pp. 649-653
    • Hoffmann, H.1    Yeager, E.2    Stuehr, J.3
  • 235
    • 0016705956 scopus 로고
    • A double beam rapid-scanning stopped-flow spectrometer
    • Hollaway, M. R., White, H.A. (1975) A double beam rapid-scanning stopped-flow spectrometer, Biochem. J. 149, 221-231.
    • (1975) Biochem. J. , vol.149 , pp. 221-231
    • Hollaway, M.R.1    White, H.A.2
  • 236
    • 84914863885 scopus 로고
    • Pressure-jump methods
    • in Weissberger, A. (ed.), J. Wiley & Sons, New York
    • Knoche, W. (1974) Pressure-jump methods, in Weissberger, A. (ed.) Techniques of Chemistry, Vol. VI, Part II, pp. 187-210, J. Wiley & Sons, New York.
    • (1974) Techniques of Chemistry , vol.VI , Issue.PART II , pp. 187-210
    • Knoche, W.1
  • 237
    • 84889328736 scopus 로고
    • Fast reactions
    • Methods Enzymol. 16
    • Kustin, K. (1969) Fast reactions, Methods Enzymol. 16.
    • (1969)
    • Kustin, K.1
  • 238
    • 0022338551 scopus 로고
    • Pressure-jump study of the kinetics of ethidium bromide binding to DNA
    • Macgregor, R. B., Clegg, R. M., Jovin, T.M. (1985) Pressure-jump study of the kinetics of ethidium bromide binding to DNA, Biochemistry 24, 5503-5510.
    • (1985) Biochemistry , vol.24 , pp. 5503-5510
    • Macgregor, R.B.1    Clegg, R.M.2    Jovin, T.M.3
  • 241
    • 33745147695 scopus 로고
    • Chemical reactions produced by very high light intensities
    • Norrish, R. G.W., Porter, G. (1949) Chemical reactions produced by very high light intensities, Nature 164, 658.
    • (1949) Nature , vol.164 , pp. 658
    • Norrish, R.G.W.1    Porter, G.2
  • 242
    • 0642294321 scopus 로고
    • Flash photolysis
    • in Weissberger, A. (ed.), J. Wiley & Sons, New York
    • Porter, G., West, M.A. (1974) Flash photolysis, in Weissberger, A. (ed.) Techniques of Chemistry, Vol. VI, Part II, pp. 367-462, J. Wiley & Sons, New York.
    • (1974) Techniques of Chemistry , vol.VI , Issue.PART II , pp. 367-462
    • Porter, G.1    West, M.A.2
  • 243
    • 84874639851 scopus 로고
    • Rapid reactions
    • in Friess, S. L., Lewis, E. S., Weissberger, A. (eds.), John Wiley & Sons, New York
    • Roughton, F. J.W., Chance, B. (1963) Rapid reactions, in Friess, S. L., Lewis, E. S., Weissberger, A. (eds.) Techniques of Organic Chemistry, Vol. VIII, Part II, pp. 703-792. John Wiley & Sons, New York.
    • (1963) Techniques of Organic Chemistry , vol.VIII , Issue.PART II , pp. 703-792
    • Roughton, F.J.W.1    Chance, B.2
  • 244
    • 33749480410 scopus 로고
    • Ein Drucksprungverfahren zur Messung der Geschwindigkeit von Ionenreaktionen
    • Stehlow, H., Becker, M. (1959) Ein Drucksprungverfahren zur Messung der Geschwindigkeit von Ionenreaktionen, Z. Elektrochem. 63, 457-461.
    • (1959) Z. Elektrochem. , vol.63 , pp. 457-461
    • Stehlow, H.1    Becker, M.2
  • 245
    • 0004159907 scopus 로고
    • Rapid Mixing and Sampling Techniques in Biochemistry
    • in Chance, B., Eisenhardt, R. M., Gibson, Q.H., Lonberg-Holm, K. K. (eds.), Academic Press, New York
    • Strittmatter, P. (1964), in Chance, B., Eisenhardt, R. M., Gibson, Q.H., Lonberg-Holm, K. K. (eds.) Rapid Mixing and Sampling Techniques in Biochemistry, p. 76. Academic Press, New York.
    • (1964) , pp. 76
    • Strittmatter, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.