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Volumn 2, Issue 5, 2006, Pages 1416-1428

Intrinsic viscosity of proteins and Platonic solids by boundary element methods

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EID: 33748472742     PISSN: 15499618     EISSN: None     Source Type: Journal    
DOI: 10.1021/ct600062y     Document Type: Article
Times cited : (24)

References (116)
  • 1
    • 0000697562 scopus 로고
    • Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride
    • Tanford, C.; Kawahara, K.; Lapanje, S. Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. J. Am. Chem. Soc. 1967, 89, 729-736.
    • (1967) J. Am. Chem. Soc , vol.89 , pp. 729-736
    • Tanford, C.1    Kawahara, K.2    Lapanje, S.3
  • 3
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of Hydrodynamic Properties of Globular Proteins from Their Atomic-Level Structure
    • Garcia de la Torre, J.; Huertas, M. L.; Carrasco, B. Calculation of Hydrodynamic Properties of Globular Proteins from Their Atomic-Level Structure. Biophys. J. 2000, 78, 719-730.
    • (2000) Biophys. J , vol.78 , pp. 719-730
    • Garcia de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 4
    • 0028806159 scopus 로고
    • Calculation of translational friction and intrinsic viscosity. I. General formulation for arbitrarily shaped particles
    • Zhou, H.-X. Calculation of translational friction and intrinsic viscosity. I. General formulation for arbitrarily shaped particles. Biophys. J. 1995, 69, 2286-2297.
    • (1995) Biophys. J , vol.69 , pp. 2286-2297
    • Zhou, H.-X.1
  • 5
    • 0028867347 scopus 로고
    • Calculation of translational friction and intrinsic viscosity. II. Application to globular proteins
    • Zhou, H.-X. Calculation of translational friction and intrinsic viscosity. II. Application to globular proteins. Biophys. J. 1995, 69, 2298-2303.
    • (1995) Biophys. J , vol.69 , pp. 2298-2303
    • Zhou, H.-X.1
  • 6
    • 0032116315 scopus 로고    scopus 로고
    • The primary electroviscous effect of rigid polyions of arbitrary shape and charge distribution
    • Allison, S. A. The primary electroviscous effect of rigid polyions of arbitrary shape and charge distribution. Macromolecules 1998, 31, 4464-4474.
    • (1998) Macromolecules , vol.31 , pp. 4464-4474
    • Allison, S.A.1
  • 7
    • 0032632003 scopus 로고    scopus 로고
    • Reynolds number transport properties of axisymmetric particles employing stick and slip boundary conditions
    • Allison, S. A. Low Reynolds number transport properties of axisymmetric particles employing stick and slip boundary conditions. Macromolecules 1999, 32, 5304-5312.
    • (1999) Macromolecules , vol.32 , pp. 5304-5312
    • Allison, S.1    Low, A.2
  • 8
    • 33748451514 scopus 로고    scopus 로고
    • Precise boundary element computation of protein transport properties: Diffusion tensors, specific volume, and hydration
    • in press
    • Aragon, S. R.; Hahn, D. K. Precise boundary element computation of protein transport properties: Diffusion tensors, specific volume, and hydration. Biophys. J. 2006, in press.
    • (2006) Biophys. J
    • Aragon, S.R.1    Hahn, D.K.2
  • 9
    • 0022701708 scopus 로고
    • On an exact starting expression for macromolecular hydrodynamic models
    • Wegener, W. A. On an exact starting expression for macromolecular hydrodynamic models. Biopolymers 1986, 25, 627-637.
    • (1986) Biopolymers , vol.25 , pp. 627-637
    • Wegener, W.A.1
  • 10
    • 0016507593 scopus 로고
    • Stokes flow past a particle of arbitrary shape: A numerical method of solution
    • Youngren, G. K.; Acrivos, A. Stokes flow past a particle of arbitrary shape: A numerical method of solution. J. Fluid Mech. 1975, 69, 377-402.
    • (1975) J. Fluid Mech , vol.69 , pp. 377-402
    • Youngren, G.K.1    Acrivos, A.2
  • 11
    • 2942560499 scopus 로고    scopus 로고
    • A precise boundary element method for macromolecular transport properties
    • Aragon, S. R. A precise boundary element method for macromolecular transport properties. J. Comput. Chem. 2004, 25, 1191-1205.
    • (2004) J. Comput. Chem , vol.25 , pp. 1191-1205
    • Aragon, S.R.1
  • 13
    • 0002276429 scopus 로고
    • The influence of Brownian motion on the viscosity of solutions
    • Simha, R. The influence of Brownian motion on the viscosity of solutions. J. Phys. Chem. 1940, 44, 25-34.
    • (1940) J. Phys. Chem , vol.44 , pp. 25-34
    • Simha, R.1
  • 14
    • 0031554728 scopus 로고    scopus 로고
    • The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution
    • Harding, S. E. The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution. Prog. Biophys. Mol. Biol. 1997, 68, 207-262.
    • (1997) Prog. Biophys. Mol. Biol , vol.68 , pp. 207-262
    • Harding, S.E.1
  • 16
    • 0017846617 scopus 로고
    • Hydrodynamic properties of macromolecular complexes. IV. Intrinsic viscosity, with application to once-broken rods and multisubunit proteins
    • Garcia de la Torre, J.; Bloomfield, V. A. Hydrodynamic properties of macromolecular complexes. IV. Intrinsic viscosity, with application to once-broken rods and multisubunit proteins. Biopolymers 1978, 17, 1605-1627.
    • (1978) Biopolymers , vol.17 , pp. 1605-1627
    • Garcia de la Torre, J.1    Bloomfield, V.A.2
  • 17
    • 84976432379 scopus 로고
    • Berichtigung zu meiner Arbeit: "Eine neue Bestimmung der Molekulardimensionen
    • Einstein, A. Berichtigung zu meiner Arbeit: "Eine neue Bestimmung der Molekulardimensionen". Ann. Phys. 1911, 34, 591-597.
    • (1911) Ann. Phys , vol.34 , pp. 591-597
    • Einstein, A.1
  • 18
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly, M. L. Analytical molecular surface calculation. J. Appl. Crystallogr. 1983, 16, 548-558.
    • (1983) J. Appl. Crystallogr , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 20
    • 0027953436 scopus 로고
    • Viscometric study of human, bovine, equine and ovine haemoglobin in aqueous solution
    • Monkos, K. Viscometric study of human, bovine, equine and ovine haemoglobin in aqueous solution. Int. J. Biol. Macromol. 1994, 16, 31-35.
    • (1994) Int. J. Biol. Macromol , vol.16 , pp. 31-35
    • Monkos, K.1
  • 21
    • 0037452560 scopus 로고    scopus 로고
    • Configurational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochrome-c by weak salt
    • Quershi, S. H.; Moza, B.; Yadav, S.; Ahmad, F. Configurational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochrome-c by weak salt. Biochemistry 2003, 42, 1684-1695.
    • (2003) Biochemistry , vol.42 , pp. 1684-1695
    • Quershi, S.H.1    Moza, B.2    Yadav, S.3    Ahmad, F.4
  • 22
    • 70449613015 scopus 로고
    • The isolation and properties of crystalline tyrosinase from neurospora
    • Fling, M.; Horowitz, N. H.; Heinemann, S. F. The isolation and properties of crystalline tyrosinase from neurospora. J. Biol. Chem. 1963, 238, 2045-2053.
    • (1963) J. Biol. Chem , vol.238 , pp. 2045-2053
    • Fling, M.1    Horowitz, N.H.2    Heinemann, S.F.3
  • 23
    • 0023393714 scopus 로고
    • A kinetic, chromatographic method for studying protein hydrodynamic behavior
    • Larew, L.; Walters, R. W. A kinetic, chromatographic method for studying protein hydrodynamic behavior. Anal. Biochem. 1987, 164, 537-546.
    • (1987) Anal. Biochem , vol.164 , pp. 537-546
    • Larew, L.1    Walters, R.W.2
  • 24
    • 0021460767 scopus 로고
    • Protein diffusion coefficient measurements by laminar flow analysis: Method and applications
    • Walters, R. W.; Graham, J. F.; Moore, R. M.; Anderson, D. J. Protein diffusion coefficient measurements by laminar flow analysis: Method and applications. Anal. Biochem. 1984, 140, 190-195.
    • (1984) Anal. Biochem , vol.140 , pp. 190-195
    • Walters, R.W.1    Graham, J.F.2    Moore, R.M.3    Anderson, D.J.4
  • 25
    • 0035983632 scopus 로고    scopus 로고
    • 2/s at 24 °C.
    • 2/s at 24 °C.
  • 26
    • 0000681244 scopus 로고
    • The effect of charge and ionic strength on the viscosity of ribonuclease
    • Buzzell, J. G.; Tanford, C. The effect of charge and ionic strength on the viscosity of ribonuclease. J. Phys. Chem. 1956, 60, 1204-1207.
    • (1956) J. Phys. Chem , vol.60 , pp. 1204-1207
    • Buzzell, J.G.1    Tanford, C.2
  • 27
    • 0015382621 scopus 로고
    • Simultaneous determination of viscosity and density of protein solutions by magnetic suspension
    • Kupke, D. W.; Hodgkins, M. G.; Beams, J. W. Simultaneous determination of viscosity and density of protein solutions by magnetic suspension. Proc. Natl. Acad. Sci. U.S.A. 1972, 69, 2258-2262.
    • (1972) Proc. Natl. Acad. Sci. U.S.A , vol.69 , pp. 2258-2262
    • Kupke, D.W.1    Hodgkins, M.G.2    Beams, J.W.3
  • 28
    • 0009722952 scopus 로고    scopus 로고
    • 2/s at 25 °C.
    • 2/s at 25 °C.
  • 29
    • 0012015424 scopus 로고
    • Osmometry and general characterization of alpha-lactalbumin
    • Wetlaufer, D. B. Osmometry and general characterization of alpha-lactalbumin. C. R. Trav. Lab. Carlsberg 1961, 32, 125-138.
    • (1961) C. R. Trav. Lab. Carlsberg , vol.32 , pp. 125-138
    • Wetlaufer, D.B.1
  • 31
    • 0010962165 scopus 로고
    • Über die berechnung der gestalt von protein- molekülen
    • Polson, A. Über die berechnung der gestalt von protein- molekülen. Kolloid Z. 1939, 88, 51-61.
    • (1939) Kolloid Z , vol.88 , pp. 51-61
    • Polson, A.1
  • 32
    • 0001523290 scopus 로고
    • Isolation of crystalline α-lactalbumin from milk
    • Gordon, W. G.; Semmett, W. F. Isolation of crystalline α-lactalbumin from milk. J. Am. Chem. Soc. 1953, 75, 328-330.
    • (1953) J. Am. Chem. Soc , vol.75 , pp. 328-330
    • Gordon, W.G.1    Semmett, W.F.2
  • 33
    • 0030947242 scopus 로고    scopus 로고
    • Concentration and temperature dependence of viscosity in lysozyme aqueous solutions
    • Monkos, K. Concentration and temperature dependence of viscosity in lysozyme aqueous solutions. Biochim. Biophys. Acta 1997, 1339, 304-310.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 304-310
    • Monkos, K.1
  • 34
    • 4644336155 scopus 로고    scopus 로고
    • Rheological study of lysozyme in dimethyl sulfoxide + water solution at 298.15 K
    • Kamiyama, T.; Morita, M.; Kimura, T. Rheological study of lysozyme in dimethyl sulfoxide + water solution at 298.15 K. J. Chem. Eng. Data 2004, 49, 1350-1353.
    • (2004) J. Chem. Eng. Data , vol.49 , pp. 1350-1353
    • Kamiyama, T.1    Morita, M.2    Kimura, T.3
  • 35
    • 33846300794 scopus 로고
    • The molecular weight and dimensions of the lysozyme molecule in solution
    • Luzzati, A.; Champagne, M. The molecular weight and dimensions of the lysozyme molecule in solution. C. R. Hebd. Seances Acad. Sci. 1957, 244, 2930-2932.
    • (1957) C. R. Hebd. Seances Acad. Sci , vol.244 , pp. 2930-2932
    • Luzzati, A.1    Champagne, M.2
  • 37
    • 33846291157 scopus 로고
    • Détermination du nombre de viscosité limite des proteins. Application aux anhydrases carboniques erythrocytaires humaines
    • Bouthier, M.; Quaranta, C.; Savary, J.; Reynaud, J. Détermination du nombre de viscosité limite des proteins. Application aux anhydrases carboniques erythrocytaires humaines. J. Chim. Phys. Phys.-Chim. Biol. 1976, 73, 776-782.
    • (1976) J. Chim. Phys. Phys.-Chim. Biol , vol.73 , pp. 776-782
    • Bouthier, M.1    Quaranta, C.2    Savary, J.3    Reynaud, J.4
  • 38
    • 36849107354 scopus 로고
    • Measurements of the rotational diffusion coefficient of lysozyme by depolarized light scattering. I. Configuration of lysozyme in solution
    • Dubin, S. B.; Clark, N. A.; Benedek, G. B. Measurements of the rotational diffusion coefficient of lysozyme by depolarized light scattering. I. Configuration of lysozyme in solution. J. Chem. Phys. 1971, 54, 5158-5164.
    • (1971) J. Chem. Phys , vol.54 , pp. 5158-5164
    • Dubin, S.B.1    Clark, N.A.2    Benedek, G.B.3
  • 39
    • 0018969935 scopus 로고
    • Viscometric parameters for myoglobin
    • Harding, S. E. Viscometric parameters for myoglobin. IRCS Med. Sci. 1980, 8, 610.
    • (1980) IRCS Med. Sci , vol.8 , pp. 610
    • Harding, S.E.1
  • 40
    • 0000304006 scopus 로고
    • Determination of molecular weights and diffusion coefficients in the ultracentrifuge
    • Ehrenberg, A. Determination of molecular weights and diffusion coefficients in the ultracentrifuge. Acta Chem. Scand. 1957, 11, 1257-1270.
    • (1957) Acta Chem. Scand , vol.11 , pp. 1257-1270
    • Ehrenberg, A.1
  • 41
    • 0015500277 scopus 로고
    • The self-diffusion coefficients of myoglobin and hemoglobin in concentrated solutions
    • Riveros-Moreno, V.; Wittenberg, J. B. The self-diffusion coefficients of myoglobin and hemoglobin in concentrated solutions. J. Biol. Chem. 1972, 247, 895-901.
    • (1972) J. Biol. Chem , vol.247 , pp. 895-901
    • Riveros-Moreno, V.1    Wittenberg, J.B.2
  • 42
    • 33846323031 scopus 로고
    • Structural transitions of soybean trypsin inhibitor. II. The denatured state in urea
    • Edelhoch, H.; Steiner, R. F. Structural transitions of soybean trypsin inhibitor. II. The denatured state in urea. J. Biol. Chem. 1963, 238, 931-938.
    • (1963) J. Biol. Chem , vol.238 , pp. 931-938
    • Edelhoch, H.1    Steiner, R.F.2
  • 43
    • 0013582869 scopus 로고    scopus 로고
    • 3.
    • 3.
  • 44
    • 1542470934 scopus 로고
    • Effect of urea on trypsin and alpha-chymotrypsin
    • Harris, J. L. Effect of urea on trypsin and alpha-chymotrypsin. Nature 1956, 177, 471-473.
    • (1956) Nature , vol.177 , pp. 471-473
    • Harris, J.L.1
  • 47
    • 33748448803 scopus 로고
    • Molecular-kinetic properties of crystalline trypsinogen
    • Tietze, F. Molecular-kinetic properties of crystalline trypsinogen. J. Biol. Chem. 1953, 204, 1-11.
    • (1953) J. Biol. Chem , vol.204 , pp. 1-11
    • Tietze, F.1
  • 48
    • 0001222935 scopus 로고
    • The molecular size and shape of the pancreatic proteases. III. α-chymotrypsin
    • Schwert, G. W.; Kaufman, S. The molecular size and shape of the pancreatic proteases. III. α-chymotrypsin. J. Biol. Chem. 1951, 190, 807-816.
    • (1951) J. Biol. Chem , vol.190 , pp. 807-816
    • Schwert, G.W.1    Kaufman, S.2
  • 49
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. Protein denaturation. Adv. Protein Chem. 1968, 23, 121-282.
    • (1968) Adv. Protein Chem , vol.23 , pp. 121-282
    • Tanford, C.1
  • 50
    • 0010470541 scopus 로고    scopus 로고
    • Schwert, G. W. The molecular size and shape of the pancreatic proteases. II. Chymotrypsinogen. J. Biol. Chem. 1951, 190, 799-806. Calculated from [η] = ξν, where ξ is the viscosity factor and ν is the partial molar
    • Schwert, G. W. The molecular size and shape of the pancreatic proteases. II. Chymotrypsinogen. J. Biol. Chem. 1951, 190, 799-806. Calculated from [η] = ξν, where ξ is the viscosity factor and ν is the partial molar volume.
  • 52
    • 0014011587 scopus 로고
    • Purification and properties of human erythrocite carbonic anhydrases
    • Armstrong, J. M.; Myers, D. V.; Verpoorte, J. A.; Edsall, J. T. Purification and properties of human erythrocite carbonic anhydrases. J. Biol. Chem. 1966, 241, 5137-5149.
    • (1966) J. Biol. Chem , vol.241 , pp. 5137-5149
    • Armstrong, J.M.1    Myers, D.V.2    Verpoorte, J.A.3    Edsall, J.T.4
  • 53
    • 0015766411 scopus 로고
    • Denaturation of bovine carbonic anhydrase b by guanidine hydrochloride. A process involving sequential conformational transitions
    • Wong, K.-P.; Tanford, C. Denaturation of bovine carbonic anhydrase b by guanidine hydrochloride. A process involving sequential conformational transitions. J. Biol. Chem. 1973, 248, 8518-8523.
    • (1973) J. Biol. Chem , vol.248 , pp. 8518-8523
    • Wong, K.-P.1    Tanford, C.2
  • 54
    • 0000973015 scopus 로고    scopus 로고
    • 3.
    • 3.
  • 55
    • 33846327016 scopus 로고
    • The effect of guanidine hydrochloride on crystalline pepsin
    • Blumenfeld, O. O.; Léonis, J.; Perlmann, G. E. The effect of guanidine hydrochloride on crystalline pepsin. J. Biol. Chem. 1960, 235, 379-382.
    • (1960) J. Biol. Chem , vol.235 , pp. 379-382
    • Blumenfeld, O.O.1    Léonis, J.2    Perlmann, G.E.3
  • 56
    • 0038860603 scopus 로고
    • The denaturation of pepsin. I. Macromolecular change
    • Edelhoch, H. The denaturation of pepsin. I. Macromolecular change. J. Am. Chem. Soc. 1957, 79, 6100-6109.
    • (1957) J. Am. Chem. Soc , vol.79 , pp. 6100-6109
    • Edelhoch, H.1
  • 57
    • 33748443947 scopus 로고
    • The shape of protein molecules. II. Viscosity and diffusion studies of native proteins
    • Neurath, H.; Cooper, G. R.; Erickson, J. O. The shape of protein molecules. II. Viscosity and diffusion studies of native proteins. J. Biol. Chem. 1941, 138, 411-436.
    • (1941) J. Biol. Chem , vol.138 , pp. 411-436
    • Neurath, H.1    Cooper, G.R.2    Erickson, J.O.3
  • 58
    • 0013966440 scopus 로고
    • Viscosity of g-ADP and g-ATP actin
    • Cohen, L. B. Viscosity of g-ADP and g-ATP actin. Arch. Biochem. Biophys. 1966, 117, 289-295.
    • (1966) Arch. Biochem. Biophys , vol.117 , pp. 289-295
    • Cohen, L.B.1
  • 59
    • 0021204075 scopus 로고
    • Detection and characterization of actin monomers, oligomers, and filaments in solution by measurement of fluorescence photobleaching recovery
    • Lanni, F.; Ware, B. R. Detection and characterization of actin monomers, oligomers, and filaments in solution by measurement of fluorescence photobleaching recovery. Biophys. J. 1984, 46, 97-110.
    • (1984) Biophys. J , vol.46 , pp. 97-110
    • Lanni, F.1    Ware, B.R.2
  • 60
    • 0021985484 scopus 로고
    • The presence of oligomers at subcritical actin concentrations
    • Newman, J.; Estes, J. E.; Selden, L. A.; Gershman, L. C. The presence of oligomers at subcritical actin concentrations. Biochemistry 1985, 24, 1538-1544.
    • (1985) Biochemistry , vol.24 , pp. 1538-1544
    • Newman, J.1    Estes, J.E.2    Selden, L.A.3    Gershman, L.C.4
  • 61
    • 26444559678 scopus 로고
    • Extent of renaturation of reduced taka-amylase a before reformation of disulfide bonds
    • Takagi, T.; Isemura, T. Extent of renaturation of reduced taka-amylase a before reformation of disulfide bonds. Biochim. Biophys. Acta 1966, 130, 233-240.
    • (1966) Biochim. Biophys. Acta , vol.130 , pp. 233-240
    • Takagi, T.1    Isemura, T.2
  • 62
    • 33748455816 scopus 로고
    • Physicochemical studies on taka-amylase a. I. Size and shape determination by the measurement of sedimentation constant, diffusion constant, and viscosity
    • Isemura, T.; Fujita, S. Physicochemical studies on taka-amylase a. I. Size and shape determination by the measurement of sedimentation constant, diffusion constant, and viscosity. J. Biochem. (Tokyo) 1957, 44, 443-450.
    • (1957) J. Biochem. (Tokyo) , vol.44 , pp. 443-450
    • Isemura, T.1    Fujita, S.2
  • 63
    • 0002829561 scopus 로고    scopus 로고
    • Molten globule-like state of human serum albumin at low pH
    • Muzammil, S.; Kumar, Y.; Tayyab, S. Molten globule-like state of human serum albumin at low pH. Eur. J. Biochem. 1999, 266, 26-32.
    • (1999) Eur. J. Biochem , vol.266 , pp. 26-32
    • Muzammil, S.1    Kumar, Y.2    Tayyab, S.3
  • 64
    • 0000888013 scopus 로고
    • Physical-chemical characteristics of certain of the proteins of normal human plasma
    • Oncley, J. L.; Scatchard, G.; Brown, A. Physical-chemical characteristics of certain of the proteins of normal human plasma. J. Phys. Colloid Chem. 1947, 51, 184-198.
    • (1947) J. Phys. Colloid Chem , vol.51 , pp. 184-198
    • Oncley, J.L.1    Scatchard, G.2    Brown, A.3
  • 65
    • 2942738911 scopus 로고    scopus 로고
    • On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach
    • Monkos, K. On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach. Biochim. Biophys. Acta 2004, 1700, 27-34.
    • (2004) Biochim. Biophys. Acta , vol.1700 , pp. 27-34
    • Monkos, K.1
  • 67
    • 0003180166 scopus 로고
    • Sedimentation and diffusion of human albumins. I. Normal human albumins at low concentration
    • Charlwood, P. A. Sedimentation and diffusion of human albumins. I. Normal human albumins at low concentration. Biochem. J. 1952, 51, 113-118.
    • (1952) Biochem. J , vol.51 , pp. 113-118
    • Charlwood, P.A.1
  • 68
    • 0010430799 scopus 로고
    • On the modification of conalbumin by acid. II. Effect of pH and salt concentration on the sedimentation behavior, viscosity and osmotic pressure of conalbumin solutions
    • Phelps, R. A.; Cann, J. R. On the modification of conalbumin by acid. II. Effect of pH and salt concentration on the sedimentation behavior, viscosity and osmotic pressure of conalbumin solutions. Arch. Biochem. Biophys. 1956, 61, 51-71.
    • (1956) Arch. Biochem. Biophys , vol.61 , pp. 51-71
    • Phelps, R.A.1    Cann, J.R.2
  • 69
    • 0032486313 scopus 로고    scopus 로고
    • 2/s at 25 °C.
    • 2/s at 25 °C.
  • 70
    • 0017707697 scopus 로고
    • Etude de la moléculaire de la lactotransferrine et de la serotransferrine humaines
    • Léger, D.; Verbert, A.; Loucheux, M.-H.; Spik, G. Etude de la moléculaire de la lactotransferrine et de la serotransferrine humaines. Ann. Biol. Anim. Biochem. Biophys. 1977, 17, 737-747.
    • (1977) Ann. Biol. Anim. Biochem. Biophys , vol.17 , pp. 737-747
    • Léger, D.1    Verbert, A.2    Loucheux, M.-H.3    Spik, G.4
  • 71
    • 0015219737 scopus 로고
    • Molecular weight, single-chain structure and amino acid composition of human lactoferrin
    • Querinjean, P.; Masson, P. L.; Heremans, J. F. Molecular weight, single-chain structure and amino acid composition of human lactoferrin. Eur. J. Biochem. 1971, 20, 420-425.
    • (1971) Eur. J. Biochem , vol.20 , pp. 420-425
    • Querinjean, P.1    Masson, P.L.2    Heremans, J.F.3
  • 72
    • 0014977439 scopus 로고
    • Bovine erythrocite cupro-zinc protein. 2. Physicochemical properties and circular dichroism
    • Wood, E.; Dalgleish, D.; Bannister, W. Bovine erythrocite cupro-zinc protein. 2. Physicochemical properties and circular dichroism. Eur. J. Biochem. 1971, 18, 187-193.
    • (1971) Eur. J. Biochem , vol.18 , pp. 187-193
    • Wood, E.1    Dalgleish, D.2    Bannister, W.3
  • 73
    • 33846282122 scopus 로고
    • Ph.D. Thesis, Iowa State University
    • Bunville, L. G. Ph.D. Thesis, Iowa State University, 1959.
    • (1959)
    • Bunville, L.G.1
  • 74
    • 0014198603 scopus 로고
    • Effect of pH on β-lactoglobulin
    • McKenzie, H. A.; Sawyer, W. H. Effect of pH on β-lactoglobulin. Nature 1967, 214, 1101-1104.
    • (1967) Nature , vol.214 , pp. 1101-1104
    • McKenzie, H.A.1    Sawyer, W.H.2
  • 75
    • 33846321352 scopus 로고
    • Osmotic pressure of β-lactoglobulin solutions
    • Bull, H. B.; Currie, B. T. Osmotic pressure of β-lactoglobulin solutions. J. Am. Chem. Soc. 1946, 68, 742-745.
    • (1946) J. Am. Chem. Soc , vol.68 , pp. 742-745
    • Bull, H.B.1    Currie, B.T.2
  • 76
    • 84987285345 scopus 로고
    • Separation of beta-lactoglobulin from other milk serum proteins by trichloroacetic acid
    • Fox, K. K.; Holsinger, V. H.; Posati, L. P.; Pallansch, M. J. Separation of beta-lactoglobulin from other milk serum proteins by trichloroacetic acid. J. Dairy Sci. 1967, 50, 1363-1367.
    • (1967) J. Dairy Sci , vol.50 , pp. 1363-1367
    • Fox, K.K.1    Holsinger, V.H.2    Posati, L.P.3    Pallansch, M.J.4
  • 77
    • 20744432646 scopus 로고
    • The Guoy diffusiometer; further calibration
    • Ogston, A. G. The Guoy diffusiometer; further calibration. Proc. R. Soc. London 1949, 196, 272-285.
    • (1949) Proc. R. Soc. London , vol.196 , pp. 272-285
    • Ogston, A.G.1
  • 78
    • 33846285516 scopus 로고
    • Investigation of the physical-chemical properties of α-chymotrypsin and its B and C chain
    • Samsonov, G. V.; Ponomareva, R. B.; Bolotina, I. A. Investigation of the physical-chemical properties of α-chymotrypsin and its B and C chain. Biofizika 1965, 10, 520-522.
    • (1965) Biofizika , vol.10 , pp. 520-522
    • Samsonov, G.V.1    Ponomareva, R.B.2    Bolotina, I.A.3
  • 79
    • 0001222935 scopus 로고
    • The molecular size and shape of the pancreatic proteases. III. α-Chymotrypsin
    • Schwert, G. W.; Kaufman, S. The molecular size and shape of the pancreatic proteases. III. α-Chymotrypsin. J. Biol. Chem. 1951, 190, 807-816.
    • (1951) J. Biol. Chem , vol.190 , pp. 807-816
    • Schwert, G.W.1    Kaufman, S.2
  • 80
    • 84984439266 scopus 로고
    • Crystalline chymo-trypsin and chymo-trypsinogen: I. Isolation, crystallization, and general properties of a new proteolytic enzyme and its precursor
    • Kunitz, M.; Northrop, J. H. Crystalline chymo-trypsin and chymo-trypsinogen: I. Isolation, crystallization, and general properties of a new proteolytic enzyme and its precursor. J. Gen. Physiol. 1935, 18, 433-458.
    • (1935) J. Gen. Physiol , vol.18 , pp. 433-458
    • Kunitz, M.1    Northrop, J.H.2
  • 82
    • 0017845114 scopus 로고
    • Sedimentation studies of the reversible dimer-tetramer transition kinetics of concanavalin A
    • Huet, M.; Claverie, J.-M. Sedimentation studies of the reversible dimer-tetramer transition kinetics of concanavalin A. Biochemistry 1978, 17, 236-241.
    • (1978) Biochemistry , vol.17 , pp. 236-241
    • Huet, M.1    Claverie, J.-M.2
  • 83
    • 0017710430 scopus 로고    scopus 로고
    • 3.
    • 3.
  • 84
    • 0023050635 scopus 로고
    • Effect of physical environment on the conformation of ricin. Influence of low pH
    • Frénoy, J.-P. Effect of physical environment on the conformation of ricin. Influence of low pH. Biochem. J. 1986, 240, 221-226.
    • (1986) Biochem. J , vol.240 , pp. 221-226
    • Frénoy, J.-P.1
  • 85
    • 16344388785 scopus 로고
    • A study of the purification and properties of ricin
    • Kabat, E. A.; Heidelberger, M.; Bezer, A. E. A study of the purification and properties of ricin. J. Biol. Chem. 1947, 168, 629-639.
    • (1947) J. Biol. Chem , vol.168 , pp. 629-639
    • Kabat, E.A.1    Heidelberger, M.2    Bezer, A.E.3
  • 86
    • 0019860003 scopus 로고
    • Oxygenation of hemoglobin: Correspondence of crystal and solution properties using translational diffusion constant measurements
    • Sanders, A. H.; Purich, D. L.; Cannell, D. S. Oxygenation of hemoglobin: Correspondence of crystal and solution properties using translational diffusion constant measurements. J. Mol. Biol. 1981, 147, 583-595.
    • (1981) J. Mol. Biol , vol.147 , pp. 583-595
    • Sanders, A.H.1    Purich, D.L.2    Cannell, D.S.3
  • 87
    • 0014149138 scopus 로고
    • Conformational states of the subunit of Escherichia coli alkaline phosphatase
    • Reynolds, J. A.; Schlesinger, M. J. Conformational states of the subunit of Escherichia coli alkaline phosphatase. Biochemistry 1967, 6, 3552-3559.
    • (1967) Biochemistry , vol.6 , pp. 3552-3559
    • Reynolds, J.A.1    Schlesinger, M.J.2
  • 88
    • 33846303319 scopus 로고    scopus 로고
    • 3.
    • 3.
  • 89
    • 0014938752 scopus 로고
    • Physicochemical characterization of citrate synthase
    • Wu, J.-Y.; Yang, J. T. Physicochemical characterization of citrate synthase. J. Biol. Chem. 1970, 24, 212-218.
    • (1970) J. Biol. Chem , vol.24 , pp. 212-218
    • Wu, J.-Y.1    Yang, J.T.2
  • 90
    • 0014940060 scopus 로고
    • Constitutive inorganic pyrophosphatase of Escherichia coli. III. Molecular weight and physical properties of the enzyme and its subunits
    • Wong, S. C. K.; Hall, D. C.; Josse, J. Constitutive inorganic pyrophosphatase of Escherichia coli. III. Molecular weight and physical properties of the enzyme and its subunits. J. Biol. Chem. 1970, 245, 4335-4341.
    • (1970) J. Biol. Chem , vol.245 , pp. 4335-4341
    • Wong, S.C.K.1    Hall, D.C.2    Josse, J.3
  • 91
    • 0014301487 scopus 로고
    • Examination of the dissociation of multichain proteins in guanidine hydrochloride by membrane osmometry
    • Castellino, J.; Barker, R. Examination of the dissociation of multichain proteins in guanidine hydrochloride by membrane osmometry. Biochemistry 1968, 7, 2207-2217.
    • (1968) Biochemistry , vol.7 , pp. 2207-2217
    • Castellino, J.1    Barker, R.2
  • 92
    • 0000435323 scopus 로고
    • The dissociation and reconstitution of aldolase
    • Stellwagen, E.; Schachman, H. K. The dissociation and reconstitution of aldolase. Biochemistry 1962, 1, 1056-1069.
    • (1962) Biochemistry , vol.1 , pp. 1056-1069
    • Stellwagen, E.1    Schachman, H.K.2
  • 93
    • 0002679956 scopus 로고
    • Aldolase dissociation into subunits by reaction with succinic anhydride
    • Hass, L. F. Aldolase dissociation into subunits by reaction with succinic anhydride. Biochemistry 1964, 3, 535-541.
    • (1964) Biochemistry , vol.3 , pp. 535-541
    • Hass, L.F.1
  • 94
    • 33748467568 scopus 로고
    • Investigation of muscular aldolase in various stages of isolation
    • Glikina, M. V.; Finogenov, P. A. Investigation of muscular aldolase in various stages of isolation. Biokhimiya 1950, 15, 457-464.
    • (1950) Biokhimiya , vol.15 , pp. 457-464
    • Glikina, M.V.1    Finogenov, P.A.2
  • 95
    • 0014530987 scopus 로고
    • Evaluation of diffusion coefficients of proteins from sedimentation boundary curves
    • Kawahara, K. Evaluation of diffusion coefficients of proteins from sedimentation boundary curves. Biochemistry 1969, 8, 2551-2557.
    • (1969) Biochemistry , vol.8 , pp. 2551-2557
    • Kawahara, K.1
  • 97
    • 0013845243 scopus 로고
    • Über die aldolase der kaninchenleber molekulargewicht, dissoziation in untereinheiten
    • Christen, P.; Göschke, H.; Leuthardt, F.; Schmid, A. Über die aldolase der kaninchenleber molekulargewicht, dissoziation in untereinheiten. Helv. Chim. Acta 1965, 48, 1050-1056.
    • (1965) Helv. Chim. Acta , vol.48 , pp. 1050-1056
    • Christen, P.1    Göschke, H.2    Leuthardt, F.3    Schmid, A.4
  • 98
    • 0000898837 scopus 로고
    • Dissociation of catalase into subunits
    • Tanford, C.; Lovrien, R. Dissociation of catalase into subunits. J. Am. Chem. Soc. 1962, 84, 1892-1896.
    • (1962) J. Am. Chem. Soc , vol.84 , pp. 1892-1896
    • Tanford, C.1    Lovrien, R.2
  • 99
    • 0001177754 scopus 로고
    • Reconstitution of acid-denatured catalase
    • Samejima, T.; Yang, J. T. Reconstitution of acid-denatured catalase. J. Biol. Chem. 1963, 238, 3256-3261.
    • (1963) J. Biol. Chem , vol.238 , pp. 3256-3261
    • Samejima, T.1    Yang, J.T.2
  • 100
    • 33748444705 scopus 로고
    • The molecular weight of crystalline catalase
    • Sumner, J.; Gralén, N. The molecular weight of crystalline catalase. Science 1938, 87, 284.
    • (1938) Science , vol.87 , pp. 284
    • Sumner, J.1    Gralén, N.2
  • 101
    • 84963084839 scopus 로고
    • Splitting of the catalase molecule by alkali treatment
    • Samejima, T. Splitting of the catalase molecule by alkali treatment. J. Biochem. 1959, 46, 155-159.
    • (1959) J. Biochem , vol.46 , pp. 155-159
    • Samejima, T.1
  • 102
    • 13344286184 scopus 로고
    • Studies on the lactose-splitting enzyme. XIII. Quantity and configuration of beta-galactosidase from E. coli
    • Sund, H.; Weber, K. Studies on the lactose-splitting enzyme. XIII. Quantity and configuration of beta-galactosidase from E. coli. Biochem. Z. 1963, 363, 24-34.
    • (1963) Biochem. Z , vol.363 , pp. 24-34
    • Sund, H.1    Weber, K.2
  • 103
    • 0017577361 scopus 로고
    • Self-association of alpha-chymotrypsin at low ionic strength in the vicinity of its pH optimum
    • Tellam, R.; Winzor, D. J. Self-association of alpha-chymotrypsin at low ionic strength in the vicinity of its pH optimum. Biochem. J. 1977, 161, 687-694.
    • (1977) Biochem. J , vol.161 , pp. 687-694
    • Tellam, R.1    Winzor, D.J.2
  • 104
    • 0023038384 scopus 로고
    • Subunit equilibria of porcine heart citrate synthase. Effects of enzyme concentration, pH, and substrates
    • McEvily, A. J.; Harrison, J. H. Subunit equilibria of porcine heart citrate synthase. Effects of enzyme concentration, pH, and substrates. J. Biol. Chem. 1986, 261, 2593-2598.
    • (1986) J. Biol. Chem , vol.261 , pp. 2593-2598
    • McEvily, A.J.1    Harrison, J.H.2
  • 106
    • 0018789696 scopus 로고
    • Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents
    • Malinowski, D. P.; Fridovich, I. Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents. Biochemistry 1979, 18, 5055-5060.
    • (1979) Biochemistry , vol.18 , pp. 5055-5060
    • Malinowski, D.P.1    Fridovich, I.2
  • 107
    • 0015495886 scopus 로고
    • Stability of quaternary structure of mammalian and avian fructose diphosphate aldolases
    • Lebherz, H. G. Stability of quaternary structure of mammalian and avian fructose diphosphate aldolases. Biochemistry 1972, 11, 2243-2250.
    • (1972) Biochemistry , vol.11 , pp. 2243-2250
    • Lebherz, H.G.1
  • 108
    • 0019889057 scopus 로고
    • Thermodynamics of concanavalin a dimer-tetramer self-association: Sedimentation equilibrium studies
    • Senear, D. F.; Teller, D. C. Thermodynamics of concanavalin a dimer-tetramer self-association: Sedimentation equilibrium studies. Biochemistry 1981, 20, 3076-3083.
    • (1981) Biochemistry , vol.20 , pp. 3076-3083
    • Senear, D.F.1    Teller, D.C.2
  • 109
    • 0001520606 scopus 로고
    • A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase
    • Garen, A.; Levinthal, C. A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase. Biochim. Biophys. Acta 1960, 38, 470-483.
    • (1960) Biochim. Biophys. Acta , vol.38 , pp. 470-483
    • Garen, A.1    Levinthal, C.2
  • 110
    • 0028049318 scopus 로고
    • Design, creation, and characterization of a stable, monomeric triosephosphate isomerase
    • Borchert, T. V.; Abagyan, R.; Jaenicke, R.; Wierenga, R. K. Design, creation, and characterization of a stable, monomeric triosephosphate isomerase. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 1515-1518.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 1515-1518
    • Borchert, T.V.1    Abagyan, R.2    Jaenicke, R.3    Wierenga, R.K.4
  • 111
    • 0014429239 scopus 로고
    • Dissociation of hemoglobin into subunits. H. Human oxyhemoglobin: Gel filtration studies
    • Chiancone, E.; Gilbert, L. M.; Gilbert, G. A.; Kellett, G. L. Dissociation of hemoglobin into subunits. H. Human oxyhemoglobin: Gel filtration studies. J. Biol. Chem. 1968, 243, 1212-1219.
    • (1968) J. Biol. Chem , vol.243 , pp. 1212-1219
    • Chiancone, E.1    Gilbert, L.M.2    Gilbert, G.A.3    Kellett, G.L.4
  • 113
    • 0026795182 scopus 로고
    • A third quaternary structure of human hemoglobin A at 1.7-Å resolutioa
    • Silva, M. M.; Rogers, P. H.; Arnone, A. A third quaternary structure of human hemoglobin A at 1.7-Å resolutioa J. Biol. Chem. 1992, 267, 17248-17256.
    • (1992) J. Biol. Chem , vol.267 , pp. 17248-17256
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 115
    • 0025007598 scopus 로고
    • High-resolution structure of horse heart cytochrome C
    • Bushnell, G. W.; Louie, G. V.; Brayer, G. D. High-resolution structure of horse heart cytochrome C. J. Mol. Biol. 1990, 214, 585-595.
    • (1990) J. Mol. Biol , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3


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