메뉴 건너뛰기




Volumn 28, Issue , 1999, Pages 75-100

Modern applications of analytical ultracentrifugation

Author keywords

Analytical ultracentrifugation; Hydrodynamics; Interacting systems; Macromolecular characterization; Thermodynamics

Indexed keywords

ANALYTIC METHOD; ARTICLE; CENTRIFUGATION; DENSITY GRADIENT CENTRIFUGATION; HYDRODYNAMICS; PRIORITY JOURNAL; SEDIMENTATION RATE; THERMODYNAMICS; VISCOSITY;

EID: 0032984921     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.28.1.75     Document Type: Article
Times cited : (241)

References (153)
  • 1
    • 84981869976 scopus 로고
    • Part VI. Chemically interacting systems II. Chemically reacting systems of the type A + B = AB, I. Sedimentation equilibrium of ideal solutions
    • 1. Adams ET Jr. 1969. Part VI. Chemically interacting systems II. Chemically reacting systems of the type A + B = AB, I. Sedimentation equilibrium of ideal solutions. Ann. NY Acad. Sci. 164:226-44
    • (1969) Ann. NY Acad. Sci. , vol.164 , pp. 226-244
    • Adams E.T., Jr.1
  • 2
    • 0013602366 scopus 로고
    • Sedimentation equilibrium in reacting systems. II. Extensions of the theory to several types of association phenomena
    • 2. Adams ET Jr, Williams JW. 1964. Sedimentation equilibrium in reacting systems. II. Extensions of the theory to several types of association phenomena. J. Am. Chem. Soc. 86:3454-61
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 3454-3461
    • Adams E.T., Jr.1    Williams, J.W.2
  • 3
    • 0027968015 scopus 로고
    • Formation of heterodimers from three neurotrophins, nerve growth factor, neurotrophin-3, and brain-derived neurotrophic factor
    • 3. Arakawa T, Haniu M, Narhi LO, Miller JA, Talvenheimo J, et al. 1994. Formation of heterodimers from three neurotrophins, nerve growth factor, neurotrophin-3, and brain-derived neurotrophic factor. J. Biol. Chem. 269:27833-39
    • (1994) J. Biol. Chem. , vol.269 , pp. 27833-27839
    • Arakawa, T.1    Haniu, M.2    Narhi, L.O.3    Miller, J.A.4    Talvenheimo, J.5
  • 4
    • 0022309432 scopus 로고
    • Calculation of the partial specific volume of proteins in concentrated salt and amino acid solutions
    • 4. Arakawa T, Timasheff SN. 1985. Calculation of the partial specific volume of proteins in concentrated salt and amino acid solutions. Methods Enzymol. 117:60-65
    • (1985) Methods Enzymol. , vol.117 , pp. 60-65
    • Arakawa, T.1    Timasheff, S.N.2
  • 5
    • 0022665926 scopus 로고
    • Technique and apparatus for automated fractionation of the contents of small centrifuge tubes: Application to analytical ultracentrifugation
    • 5. Attri AK, Minton AP. 1986. Technique and apparatus for automated fractionation of the contents of small centrifuge tubes: application to analytical ultracentrifugation. Anal. Biochem. 152:319-28
    • (1986) Anal. Biochem. , vol.152 , pp. 319-328
    • Attri, A.K.1    Minton, A.P.2
  • 6
    • 0023268035 scopus 로고
    • Simultaneous determination of the individual concentration gradients of two solute species in a centrifuged mixture: Application to analytical ultracentrifugation
    • 6. Attri AK, Minton AP. 1987. Simultaneous determination of the individual concentration gradients of two solute species in a centrifuged mixture: application to analytical ultracentrifugation. Anal. Biochem. 162:409-19
    • (1987) Anal. Biochem. , vol.162 , pp. 409-419
    • Attri, A.K.1    Minton, A.P.2
  • 7
    • 0031029481 scopus 로고    scopus 로고
    • Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles
    • 7. Behlke J, Ristau O. 1997. Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles. Biophys. J. 72:428-34
    • (1997) Biophys. J. , vol.72 , pp. 428-434
    • Behlke, J.1    Ristau, O.2
  • 10
    • 85001812599 scopus 로고
    • Polyelectrolyte charge corrected molecular weight and effective charge by sedimentation
    • 10. Braswell EH. 1987. Polyelectrolyte charge corrected molecular weight and effective charge by sedimentation. Biophys. J. 51:273-81
    • (1987) Biophys. J. , vol.51 , pp. 273-281
    • Braswell, E.H.1
  • 12
    • 0020170793 scopus 로고
    • Theory of sedimentation for ligand-mediated heterogeneous association-dissociation reactions
    • 12. Cann JR. 1982. Theory of sedimentation for ligand-mediated heterogeneous association-dissociation reactions. Biophys. Chem. 16:41-49
    • (1982) Biophys. Chem. , vol.16 , pp. 41-49
    • Cann, J.R.1
  • 14
    • 77956752195 scopus 로고
    • Thermodynamic analysis of multicomponent solutions
    • 14. Casassa EF, Eisenberg H. 1964. Thermodynamic analysis of multicomponent solutions. Adv. Protein Chem. 19:287-395
    • (1964) Adv. Protein Chem. , vol.19 , pp. 287-395
    • Casassa, E.F.1    Eisenberg, H.2
  • 15
    • 0023322946 scopus 로고
    • Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins
    • 15. Chatelier RC, Minton AP. 1987. Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins. Biopolymers 26:507-24
    • (1987) Biopolymers , vol.26 , pp. 507-524
    • Chatelier, R.C.1    Minton, A.P.2
  • 16
    • 0023369557 scopus 로고
    • Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. II. Two protein components
    • 16. Chatelier RC, Minton AP. 1987. Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. II. Two protein components. Biopolymers 26:1097-1113
    • (1987) Biopolymers , vol.26 , pp. 1097-1113
    • Chatelier, R.C.1    Minton, A.P.2
  • 17
    • 0029970884 scopus 로고    scopus 로고
    • Adsorption of globular proteins on locally planar surfaces: Models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria
    • 17. Chatelier RC, Minton AP. 1996. Adsorption of globular proteins on locally planar surfaces: models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria. Biophys. J. 71:2367-74
    • (1996) Biophys. J. , vol.71 , pp. 2367-2374
    • Chatelier, R.C.1    Minton, A.P.2
  • 18
    • 0031646705 scopus 로고    scopus 로고
    • Sedimentation velocity analysis methods: What, when and why?
    • In press
    • 18. Correia JJ. 1999. Sedimentation velocity analysis methods: What, when and why? ChemTracts: Biochem. Mol. Biol. 11:In press
    • (1999) Chemtracts: Biochem. Mol. Biol. , vol.11
    • Correia, J.J.1
  • 19
    • 0017193544 scopus 로고
    • Numerical study of the Johnston-Ogston effect in two-component systems
    • 19. Correia JJ, Johnson ML, Weiss GH, Yphantis DA. 1976. Numerical study of the Johnston-Ogston effect in two-component systems. Biophys. Chem. 5: 255-64
    • (1976) Biophys. Chem. , vol.5 , pp. 255-264
    • Correia, J.J.1    Johnson, M.L.2    Weiss, G.H.3    Yphantis, D.A.4
  • 21
    • 0013789750 scopus 로고
    • Viscocity and sedimentation of the DNA from bacteriophages T2 and T7 and the relation to molecular weight
    • 21. Crothers DM, Zimm BH. 1965. Viscocity and sedimentation of the DNA from bacteriophages T2 and T7 and the relation to molecular weight. J. Mol. Biol. 12:525-36
    • (1965) J. Mol. Biol. , vol.12 , pp. 525-536
    • Crothers, D.M.1    Zimm, B.H.2
  • 22
    • 0027410312 scopus 로고
    • Rapid and accurate microfractionation of the contents of small centrifuge tubes: Application in the measurement of molecular weight of proteins via sedimentation equilibrium
    • 22. Darawshe S, Rivas GA, Minton AP. 1993. Rapid and accurate microfractionation of the contents of small centrifuge tubes: application in the measurement of molecular weight of proteins via sedimentation equilibrium. Anal. Biochem. 209:130-35
    • (1993) Anal. Biochem. , vol.209 , pp. 130-135
    • Darawshe, S.1    Rivas, G.A.2    Minton, A.P.3
  • 23
    • 0002033301 scopus 로고
    • Sedimentation coefficients of complex biological particles
    • ed. AJ Rowe, SE Harding, JC Horton. Cambridge, UK: R. Soc. Chem.
    • 23. De La Torre JG. 1992. Sedimentation coefficients of complex biological particles. In Analytical Ultracentrifugation in Biochemistry and Polymer Science, ed. AJ Rowe, SE Harding, JC Horton, pp. 333-45. Cambridge, UK: R. Soc. Chem.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 333-345
    • De La Torre, J.G.1
  • 24
    • 0019526265 scopus 로고
    • Hydrodynamic properties of complex, rigid, biological macromolecules: Theory and applications
    • 24. De La Torre JG, Bloomfield VA. 1981. Hydrodynamic properties of complex, rigid, biological macromolecules: theory and applications. Q. Rev. Biophys. 14:81-139
    • (1981) Q. Rev. Biophys. , vol.14 , pp. 81-139
    • De La Torre, J.G.1    Bloomfield, V.A.2
  • 25
    • 0031020113 scopus 로고    scopus 로고
    • Identification and interpretation of complexity in sedimentation velocity boundaries
    • 25. Demeler B, Saber H, Hansen JC. 1997. Identification and interpretation of complexity in sedimentation velocity boundaries. Biophys. J. 72:397-407
    • (1997) Biophys. J. , vol.72 , pp. 397-407
    • Demeler, B.1    Saber, H.2    Hansen, J.C.3
  • 26
    • 84984086797 scopus 로고
    • Numerical solutions of the Lamm equation. I. Numerical procedure
    • 26. Dishon M, Weiss GH, Yphantis DA. 1966. Numerical solutions of the Lamm equation. I. Numerical procedure. Biopolymers 4:449-55
    • (1966) Biopolymers , vol.4 , pp. 449-455
    • Dishon, M.1    Weiss, G.H.2    Yphantis, D.A.3
  • 27
    • 84984086661 scopus 로고
    • Numerical solutions of the Lamm equation. II. Equilibrium sedimentation
    • 27. Dishon M, Weiss GH, Yphantis DA. 1966. Numerical solutions of the Lamm equation. II. Equilibrium sedimentation. Biopolymers 4:457-68
    • (1966) Biopolymers , vol.4 , pp. 457-468
    • Dishon, M.1    Weiss, G.H.2    Yphantis, D.A.3
  • 28
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • ed. H-J Hinz. Berlin-Heidelberg: Springer-Verlag
    • 28. Durchschlag H. 1986. Specific volumes of biological macromolecules and some other molecules of biological interest. In Thermodynamic Data for Biochemistry and Biotechnology, ed. H-J Hinz, pp. 45-128. Berlin-Heidelberg: Springer-Verlag
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45-128
    • Durchschlag, H.1
  • 29
    • 0013623497 scopus 로고
    • Determination of the partial specific volume of conjugated proteins
    • 29. Durchschlag H. 1989. Determination of the partial specific volume of conjugated proteins. Colloid Polym. Sci. 267:1139-50
    • (1989) Colloid Polym. Sci. , vol.267 , pp. 1139-1150
    • Durchschlag, H.1
  • 30
    • 0020484055 scopus 로고
    • Partial specific volume changes of proteins densimetric studies
    • 30. Durchschlag H, Jaenicke R. 1982. Partial specific volume changes of proteins densimetric studies. Biochem. Biophys. Res. Commun. 108:1047-79
    • (1982) Biochem. Biophys. Res. Commun. , vol.108 , pp. 1047-1079
    • Durchschlag, H.1    Jaenicke, R.2
  • 31
    • 0014216034 scopus 로고
    • The simultaneous determination of partial specific volumes and molecular weights with microgram quantities
    • 31. Edelstein SJ, Schachman HK. 1967. The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. J. Biol. Chem. 242:2:306-11
    • (1967) J. Biol. Chem. , vol.242 , Issue.2 , pp. 306-311
    • Edelstein, S.J.1    Schachman, H.K.2
  • 34
    • 0002922626 scopus 로고
    • Notes on the derivation of sedimentation equilibrium equations
    • ed. TM Schuster, TM Laue. Boston: Birkhauser
    • 34. Fujita H. 1994. Notes on the derivation of sedimentation equilibrium equations. In Modern Analytical Ultracentrifugation, ed. TM Schuster, TM Laue, pp. 3-14. Boston: Birkhauser
    • (1994) Modern Analytical Ultracentrifugation , pp. 3-14
    • Fujita, H.1
  • 35
    • 8644270952 scopus 로고
    • Sedimentation in the ultracentrifuge
    • 35. Goldberg RJ. 1953. Sedimentation in the ultracentrifuge. J. Phys. Chem. 57:194-202
    • (1953) J. Phys. Chem. , vol.57 , pp. 194-202
    • Goldberg, R.J.1
  • 36
    • 0028838794 scopus 로고
    • Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase
    • 36. Hall DR, Jacobsen MP, Winzor DJ. 1995. Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase. Biophys. Chem. 57:47-54
    • (1995) Biophys. Chem. , vol.57 , pp. 47-54
    • Hall, D.R.1    Jacobsen, M.P.2    Winzor, D.J.3
  • 38
    • 0028149245 scopus 로고
    • Analytical ultracentrifugation of complex macromolecular systems
    • 38. Hansen JC, Lebowitz J, Demeler B. 1994. Analytical ultracentrifugation of complex macromolecular systems. Biochemistry 33:13155-63
    • (1994) Biochemistry , vol.33 , pp. 13155-13163
    • Hansen, J.C.1    Lebowitz, J.2    Demeler, B.3
  • 39
    • 0001309448 scopus 로고
    • A general method for modeling macromolecular shape in solution. A graphical (II-G) intersection procedure for triaxial ellipsoids
    • 39. Harding SE. 1987. A general method for modeling macromolecular shape in solution. A graphical (II-G) intersection procedure for triaxial ellipsoids. Biophys. J. 51:673-80
    • (1987) Biophys. J. , vol.51 , pp. 673-680
    • Harding, S.E.1
  • 40
    • 0002331258 scopus 로고
    • Modelling the gross conformation of assemblies using hydrodynamics: The whole body approach
    • ed. SE Harding, AJ Rowe. London: R. Soc. London
    • 40. Harding SE. 1989. Modelling the gross conformation of assemblies using hydrodynamics: the whole body approach. In Dynamic Properties of Biomolecular Assemblies, ed. SE Harding, AJ Rowe. London: R. Soc. London
    • (1989) Dynamic Properties of Biomolecular Assemblies
    • Harding, S.E.1
  • 41
    • 0028138012 scopus 로고
    • Determination of macromolecular homogeneity, shape, and interactions using sedimentation velocity analytical ultracentrifugation
    • Microscopy, Optical Spectroscopy, and Macroscopic Techniques, ed. C Jones, B Mulloy, AH Thomas. Totowa, NJ: Humana
    • 41. Harding SE. 1994. Determination of macromolecular homogeneity, shape, and interactions using sedimentation velocity analytical ultracentrifugation. In Methods in Molecular Biology, Vol. 22. Microscopy, Optical Spectroscopy, and Macroscopic Techniques, ed. C Jones, B Mulloy, AH Thomas, pp. 61-73. Totowa, NJ: Humana
    • (1994) Methods in Molecular Biology , vol.22 , pp. 61-73
    • Harding, S.E.1
  • 42
    • 0030297794 scopus 로고    scopus 로고
    • Physicochemical studies on Xylinan (acetan). III. Hydrodynamic characterization by analytical ultracentrifugation and dynamic light scattering
    • 42. Harding SE, Berth G, Hartmann J, Jumel K, Colfen H, et al. 1996. Physicochemical studies on Xylinan (acetan). III. Hydrodynamic characterization by analytical ultracentrifugation and dynamic light scattering. Biopolymers 39:729-36
    • (1996) Biopolymers , vol.39 , pp. 729-736
    • Harding, S.E.1    Berth, G.2    Hartmann, J.3    Jumel, K.4    Colfen, H.5
  • 43
    • 0022351381 scopus 로고
    • The concentration-dependence of macromolecular parameters
    • 43. Harding SE, Johnson P. 1985. The concentration-dependence of macromolecular parameters. Biochem. J. 231:543-47
    • (1985) Biochem. J. , vol.231 , pp. 543-547
    • Harding, S.E.1    Johnson, P.2
  • 45
    • 0013574551 scopus 로고
    • The effects of pressure in ultracentrifugation of interacting systems
    • 45. Harrington WF. 1975, The effects of pressure in ultracentrifugation of interacting systems. Fractions 1:10-18
    • (1975) Fractions , vol.1 , pp. 10-18
    • Harrington, W.F.1
  • 46
    • 0014955681 scopus 로고
    • Exponential analysis of concentration or concentration difference data for discrete molecular weight distributions in sedimentation equilibrium
    • 46. Haschemeyer RH, Bowers WF. 1970. Exponential analysis of concentration or concentration difference data for discrete molecular weight distributions in sedimentation equilibrium. Biochemistry 9:435-45
    • (1970) Biochemistry , vol.9 , pp. 435-445
    • Haschemeyer, R.H.1    Bowers, W.F.2
  • 47
    • 0000198303 scopus 로고
    • An approximate solution to the Lamm equation
    • 47. Holladay LA. 1979. An approximate solution to the Lamm equation, Biophys. Chem. 10:187-90
    • (1979) Biophys. Chem. , vol.10 , pp. 187-190
    • Holladay, L.A.1
  • 48
    • 0013602368 scopus 로고
    • Molecular weights from approach-to-sedimentation equilibrium datausing nonlinear regression analysis
    • 48. Holladay LA. 1979. Molecular weights from approach-to-sedimentation equilibrium datausing nonlinear regression analysis. Biophys. Chem. 10:183-85
    • (1979) Biophys. Chem. , vol.10 , pp. 183-185
    • Holladay, L.A.1
  • 49
    • 0001112327 scopus 로고
    • Simultaneous rapid estimation of sedimentation coefficient and molecular weight
    • 49. Holladay LA. 1980. Simultaneous rapid estimation of sedimentation coefficient and molecular weight. Biophys. Chem. 11:303-8
    • (1980) Biophys. Chem. , vol.11 , pp. 303-308
    • Holladay, L.A.1
  • 50
    • 0015522414 scopus 로고
    • Nonideal associating systems. Documentation of a new method for determining the parameters from sedimentation equilibrium data
    • 50. HoILaday LA, Sophianopoulos AJ. 1972. Nonideal associating systems. Documentation of a new method for determining the parameters from sedimentation equilibrium data. J. Biol. Chem. 247:427-39
    • (1972) J. Biol. Chem. , vol.247 , pp. 427-439
    • Holladay, L.A.1    Sophianopoulos, A.J.2
  • 51
    • 0015963149 scopus 로고
    • Statistical evaluation of ways to analyze nonideal systems by sedimentation equilibrium
    • 51. Holladay LA, Sophianopoulos AJ. 1974. Statistical evaluation of ways to analyze nonideal systems by sedimentation equilibrium. Anal. Biochem. 57:506-28
    • (1974) Anal. Biochem. , vol.57 , pp. 506-528
    • Holladay, L.A.1    Sophianopoulos, A.J.2
  • 52
    • 0031675898 scopus 로고    scopus 로고
    • Analysis of heteroassociating systems by sedimentation equilibrium
    • In press
    • 52. Hewlett GJ. 1999. Analysis of heteroassociating systems by sedimentation equilibrium. Chem Tracts: Biochem. Mol. Biol. 11:In press
    • (1999) Chem Tracts: Biochem. Mol. Biol. , vol.11
    • Hewlett, G.J.1
  • 53
    • 0013574779 scopus 로고
    • The effects of pressure on the sedimentation equilibrium of chemically reacting systems
    • 53. Hewlett GJ, Jeffrey PD, Nichol LW. 1970. The effects of pressure on the sedimentation equilibrium of chemically reacting systems. J. Phys. Chem. 74:3607-10
    • (1970) J. Phys. Chem. , vol.74 , pp. 3607-3610
    • Hewlett, G.J.1    Jeffrey, P.D.2    Nichol, L.W.3
  • 54
    • 0026115704 scopus 로고
    • A strategy for efficient characterization of macromolecular heteroassociations via measurement of sedimentation equilibrium
    • 54. Hsu CS, Minton AP. 1991. A strategy for efficient characterization of macromolecular heteroassociations via measurement of sedimentation equilibrium. J. Mol. Recognit. 4:93-104
    • (1991) J. Mol. Recognit. , vol.4 , pp. 93-104
    • Hsu, C.S.1    Minton, A.P.2
  • 56
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • 56. Johnson ML, Correria JJ, Yphantis DA, Halvorson HR. 1981. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36:575-88
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correria, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 58
    • 0001357930 scopus 로고
    • A boundary anomaly found in the ultracentrifugal sedimentation of mixtures
    • 58. Johnston JP, Ogston AG. 1946. A boundary anomaly found in the ultracentrifugal sedimentation of mixtures. Trans. Faraday Soc. 42:789-99
    • (1946) Trans. Faraday Soc. , vol.42 , pp. 789-799
    • Johnston, J.P.1    Ogston, A.G.2
  • 59
    • 0014010861 scopus 로고
    • Viscosity and density of aqueous solutions of urea and guanidine hydrochloride
    • 59. Kawahara K, Tanford C. 1966. Viscosity and density of aqueous solutions of urea and guanidine hydrochloride. J. Biol. Chem. 241:3228-32
    • (1966) J. Biol. Chem. , vol.241 , pp. 3228-3232
    • Kawahara, K.1    Tanford, C.2
  • 60
    • 0013574408 scopus 로고
    • Convection induced by hydrostatic pressure in sedimentation velocity experiments
    • 60. Kegeles G. 1969. Convection induced by hydrostatic pressure in sedimentation velocity experiments. Biopolymers 7:83-86
    • (1969) Biopolymers , vol.7 , pp. 83-86
    • Kegeles, G.1
  • 61
    • 84981864820 scopus 로고
    • The effects of pressure in high-speed ultracentrifugation of chemically reacting systems
    • 61. Kegeles G, Kaplan S, Rhodes L. 1969. The effects of pressure in high-speed ultracentrifugation of chemically reacting systems. Ann. NY Acad. Sci. 164:183-91
    • (1969) Ann. NY Acad. Sci. , vol.164 , pp. 183-191
    • Kegeles, G.1    Kaplan, S.2    Rhodes, L.3
  • 64
    • 0029118618 scopus 로고
    • Sedimentation equilibrium as a thermodynamic tool
    • ed. GK Ackers, ML Johnson. New York: Academic
    • 64. Laue TM. 1995. Sedimentation equilibrium as a thermodynamic tool. In Methods in Enzymology, ed. GK Ackers, ML Johnson, pp. 427-52. New York: Academic
    • (1995) Methods in Enzymology , pp. 427-452
    • Laue, T.M.1
  • 66
    • 0031389509 scopus 로고    scopus 로고
    • Prototype fluorimeter for the XLA/XLI analytical ultracentrifuge
    • ed. EJ Cohn, SA Soper. Bellingham, WA: SPIE
    • 66. Laue TM, Anderson AL, Weber BJ. 1997. Prototype fluorimeter for the XLA/XLI analytical ultracentrifuge. In Ultrasensitive Biochemical Diagnostics II, ed. EJ Cohn, SA Soper, pp. 196-204. Bellingham, WA: SPIE
    • (1997) Ultrasensitive Biochemical Diagnostics II , pp. 196-204
    • Laue, T.M.1    Anderson, A.L.2    Weber, B.J.3
  • 67
    • 0021367786 scopus 로고
    • Structure of bovine blood coagulation factor Va. Determination of the subunit associations, molecular weights, and asymmetries by analytical ultracentrifugation
    • 67. Laue TM, Johnson AE, Esmon CT, Yphantis DA. 1984. Structure of bovine blood coagulation factor Va. Determination of the subunit associations, molecular weights, and asymmetries by analytical ultracentrifugation. Biochemistry 23:1339-48
    • (1984) Biochemistry , vol.23 , pp. 1339-1348
    • Laue, T.M.1    Johnson, A.E.2    Esmon, C.T.3    Yphantis, D.A.4
  • 68
    • 0027537906 scopus 로고
    • 5-Hydroxytryptophan as a new intrinsic probe for investigating protein-DNA interactions by analytical ultracentrifugation. Study of the effect of DNA on self-assembly of the bacteriophage cI repressor
    • 68. Laue TM, Scnear DF, Eaton SF, Ross JBA. 1993. 5-Hydroxytryptophan as a new intrinsic probe for investigating protein-DNA interactions by analytical ultracentrifugation. Study of the effect of DNA on self-assembly of the bacteriophage cI repressor. Biochemistry 32:2469-72
    • (1993) Biochemistry , vol.32 , pp. 2469-2472
    • Laue, T.M.1    Scnear, D.F.2    Eaton, S.F.3    Ross, J.B.A.4
  • 70
    • 0029618782 scopus 로고
    • MyoD forms micelles which can dissociate to form heterodimers with E47: Implications of micellization on function
    • 70. Laue TM, Starovasnik MA, Weintraub H, Sun X, Snider L, et al. 1995. MyoD forms micelles which can dissociate to form heterodimers with E47: implications of micellization on function. Proc. Natl. Acad. Sci. USA 92:11824-28
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11824-11828
    • Laue, T.M.1    Starovasnik, M.A.2    Weintraub, H.3    Sun, X.4    Snider, L.5
  • 71
    • 0021764714 scopus 로고
    • Rapid precision interferometry for the analytical ultracentrifuge III. Determination of period of rotation, frequency of rotation, and elapsed time
    • 71. Laue TM, Yphantis DA, Rhodes DG. 1984. Rapid precision interferometry for the analytical ultracentrifuge III. Determination of period of rotation, frequency of rotation, and elapsed time. Anal. Biochem. 143:103-12
    • (1984) Anal. Biochem. , vol.143 , pp. 103-112
    • Laue, T.M.1    Yphantis, D.A.2    Rhodes, D.G.3
  • 72
    • 0015950174 scopus 로고
    • Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride
    • 72. Lee JC, Timasheff SN. 1974. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry 13: 257-65
    • (1974) Biochemistry , vol.13 , pp. 257-265
    • Lee, J.C.1    Timasheff, S.N.2
  • 73
    • 0025874709 scopus 로고
    • Preferential assembly of the tropomyosin heterodimer: Equilibrium studies
    • 73. Lehrer SS, Stafford WF. 1991. Preferential assembly of the tropomyosin heterodimer: equilibrium studies. Biochemistry 30:5682-88
    • (1991) Biochemistry , vol.30 , pp. 5682-5688
    • Lehrer, S.S.1    Stafford, W.F.2
  • 74
    • 0000590589 scopus 로고
    • Ultracentrifugal analysis of a mixed association
    • 74. Lewis MS. 1991. Ultracentrifugal analysis of a mixed association. Biochemistry 30:11707-19
    • (1991) Biochemistry , vol.30 , pp. 11707-11719
    • Lewis, M.S.1
  • 75
    • 0028073482 scopus 로고
    • The self-association of biglycan from bovine articular cartilage
    • 75. Liu J, Laue TM, Choi HU, Tang LH, Rosenberg LC. 1994. The self-association of biglycan from bovine articular cartilage. J. Biol. Chem. 269:28366-73
    • (1994) J. Biol. Chem. , vol.269 , pp. 28366-28373
    • Liu, J.1    Laue, T.M.2    Choi, H.U.3    Tang, L.H.4    Rosenberg, L.C.5
  • 76
    • 0029117815 scopus 로고
    • Characterization of complex formation by humanized antí-IgE monoclonal antibody and monoclonal human IgE
    • 76. Liu J, Lester P, Builder S, Shire SJ. 1995. Characterization of complex formation by humanized antí-IgE monoclonal antibody and monoclonal human IgE. Biochemistry 34:10474-82
    • (1995) Biochemistry , vol.34 , pp. 10474-10482
    • Liu, J.1    Lester, P.2    Builder, S.3    Shire, S.J.4
  • 77
    • 0029020164 scopus 로고
    • Binding of vinblastine to phosphocellulose-purified and AB-class III tubulin: The role of nucleotides and beta-tubulin isotypes
    • 77. Lobert S, Frankfurter A, Correia JJ. 1995. Binding of vinblastine to phosphocellulose-purified and AB-class III tubulin: the role of nucleotides and beta-tubulin isotypes. Biochemistry 34: 8050-60
    • (1995) Biochemistry , vol.34 , pp. 8050-8060
    • Lobert, S.1    Frankfurter, A.2    Correia, J.J.3
  • 78
    • 0028287275 scopus 로고
    • Interaction of tubulin and microtubule proteins with vanadate oligomers
    • 78. Lobert S, Isern N, Hennington BS, Correia JJ. 1994. Interaction of tubulin and microtubule proteins with vanadate oligomers. Biochemistry 33:6244-52
    • (1994) Biochemistry , vol.33 , pp. 6244-6252
    • Lobert, S.1    Isern, N.2    Hennington, B.S.3    Correia, J.J.4
  • 79
    • 0030008570 scopus 로고    scopus 로고
    • Interaction of vinca alkaloids with tubulin: A comparison of vinblastine, vincristine, and vinorelbine
    • 79. Lobert S, Vulevic B, Correia JJ. 1996. Interaction of vinca alkaloids with tubulin: a comparison of vinblastine, vincristine, and vinorelbine. Biochemistry 35:6806-14
    • (1996) Biochemistry , vol.35 , pp. 6806-6814
    • Lobert, S.1    Vulevic, B.2    Correia, J.J.3
  • 80
    • 0024582038 scopus 로고
    • Interaction of clotting factor V heavy chain with prothrombin and prethrombin 1 and role of activated protein C in regulating this interaction: Analysis by analytical ultracentrifugation
    • 80. Luckow EA, Lyons DA, Ridgeway TM, Esmon CT, Laue TM. 1989. Interaction of clotting factor V heavy chain with prothrombin and prethrombin 1 and role of activated protein C in regulating this interaction: analysis by analytical ultracentrifugation. Biochemistry 28:5:2348-54
    • (1989) Biochemistry , vol.28 , Issue.5 , pp. 2348-2354
    • Luckow, E.A.1    Lyons, D.A.2    Ridgeway, T.M.3    Esmon, C.T.4    Laue, T.M.5
  • 81
    • 0025747903 scopus 로고
    • Density determination by analytical ultracentrifugation in a rapid dynamical gradient: Application to lipid and detergent aggregates containing proteins
    • 81. Lustig A, Engel A, Zulauf M. 1991. Density determination by analytical ultracentrifugation in a rapid dynamical gradient: application to lipid and detergent aggregates containing proteins. Biochim. Biophys. Acta 1115:89-95
    • (1991) Biochim. Biophys. Acta , vol.1115 , pp. 89-95
    • Lustig, A.1    Engel, A.2    Zulauf, M.3
  • 82
    • 0026547086 scopus 로고
    • Simulation of the time course of macromolecular separations in an ultracentrifuge. II. Controlling the solute concentrations
    • 82. Marque J. 1992. Simulation of the time course of macromolecular separations in an ultracentrifuge. II. Controlling the solute concentrations. Biophys. Chem. 42: 23-27
    • (1992) Biophys. Chem. , vol.42 , pp. 23-27
    • Marque, J.1
  • 83
    • 36149016757 scopus 로고
    • The settling of small particles in a fluid
    • 83. Mason M, Weaver W. 1924. The settling of small particles in a fluid. Phys. Rev. 23:412-26
    • (1924) Phys. Rev. , vol.23 , pp. 412-426
    • Mason, M.1    Weaver, W.2
  • 84
    • 0000113726 scopus 로고
    • Specific volumes of proteins and the relationship to their amino acid contents
    • 84. McMeekin TL, Marshall K. 1952. Specific volumes of proteins and the relationship to their amino acid contents. Science 116:142-44
    • (1952) Science , vol.116 , pp. 142-144
    • McMeekin, T.L.1    Marshall, K.2
  • 86
    • 0030801897 scopus 로고    scopus 로고
    • Soluble monomeric P-selectin containing only the lectin and epidermal growth factor domains binds to P-selectin glycoprotein ligand-1 on leukocytes
    • 86. Mehta P, Patel KD, Laue TM, Erickson HP, McEver RP. 1997. Soluble monomeric P-selectin containing only the lectin and epidermal growth factor domains binds to P-selectin glycoprotein ligand-1 on leukocytes. Blood 90:2381-89
    • (1997) Blood , vol.90 , pp. 2381-2389
    • Mehta, P.1    Patel, K.D.2    Laue, T.M.3    Erickson, H.P.4    McEver, R.P.5
  • 87
    • 0025169221 scopus 로고
    • Ouantitative characterization of reversible molecular associations via analytical centrifugation
    • 87. Minton AP. 1990. Ouantitative characterization of reversible molecular associations via analytical centrifugation. Anal. Biochem. 190:1-6
    • (1990) Anal. Biochem. , vol.190 , pp. 1-6
    • Minton, A.P.1
  • 88
    • 0026544299 scopus 로고
    • Simulation of the time course of macromolecular separations in an ultracentrifuge. I. Formation of a cesium chloride density gradient at 25 degrees C
    • 88. Minton AP. 1992. Simulation of the time course of macromolecular separations in an ultracentrifuge. I. Formation of a cesium chloride density gradient at 25 degrees C. Biophys. Chem. 42:13-21
    • (1992) Biophys. Chem. , vol.42 , pp. 13-21
    • Minton, A.P.1
  • 89
    • 0027829616 scopus 로고
    • Macromolecular crowding and molecular recognition
    • 89. Minton AP. 1993. Macromolecular crowding and molecular recognition. J. Mal. Recognit. 6:211-14
    • (1993) J. Mal. Recognit. , vol.6 , pp. 211-214
    • Minton, A.P.1
  • 90
    • 0028822574 scopus 로고
    • A molecular model for the dependence of the osmotic pressure of bovine serum albumin upon concentration and pH
    • 90. Minton AP. 1995. A molecular model for the dependence of the osmotic pressure of bovine serum albumin upon concentration and pH. Biophys. Chem. 57:65-70
    • (1995) Biophys. Chem. , vol.57 , pp. 65-70
    • Minton, A.P.1
  • 91
    • 0003300676 scopus 로고    scopus 로고
    • Alternative strategies for the characterization of associations via measurement of sedimentation equilibrium
    • 91. Minton AP. 1997. Alternative strategies for the characterization of associations via measurement of sedimentation equilibrium. Prog. Colloid Polym. Sci. 107:11-19
    • (1997) Prog. Colloid Polym. Sci. , vol.107 , pp. 11-19
    • Minton, A.P.1
  • 93
    • 0022155828 scopus 로고
    • Determination of the parameters of self-association by direct fitting of the omega function
    • 93. Morris M, Ralston GB. 1985. Determination of the parameters of self-association by direct fitting of the omega function. Biophys. Chem. 23:49-61
    • (1985) Biophys. Chem. , vol.23 , pp. 49-61
    • Morris, M.1    Ralston, G.B.2
  • 94
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zippers from Fos and Jun
    • 94. O'shea EK, Rutkowski R, Stafford WF, Kim PS. 1989. Preferential heterodimer formation by isolated leucine zippers from Fos and Jun. Science 245:646-48
    • (1989) Science , vol.245 , pp. 646-648
    • O'shea, E.K.1    Rutkowski, R.2    Stafford, W.F.3    Kim, P.S.4
  • 95
    • 0013603846 scopus 로고
    • On the variation of the sedimentation rate of spherical particles with concentration
    • 95. Ogston AC. 1961. On the variation of the sedimentation rate of spherical particles with concentration. J. Am. Chem. Soc. 65:51-53
    • (1961) J. Am. Chem. Soc. , vol.65 , pp. 51-53
    • Ogston, A.C.1
  • 96
    • 0026610497 scopus 로고
    • Ca2+ depedence of the interactions between protein C, thrombin, and the elastase fragment of thrombomodulin. Analysis by ultracentrifugation
    • 96. Olsen PH, Esmon NL, Esmon CT, Laue TM. 1992. Ca2+ depedence of the interactions between protein C, thrombin, and the elastase fragment of thrombomodulin. Analysis by ultracentrifugation. Biochemistry 31:746-54
    • (1992) Biochemistry , vol.31 , pp. 746-754
    • Olsen, P.H.1    Esmon, N.L.2    Esmon, C.T.3    Laue, T.M.4
  • 97
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • 97. Perkins SJ. 1986. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157:169-80
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 98
    • 0031036440 scopus 로고    scopus 로고
    • New modified Fujita-MacCosham solution for species of molecular weight <10,000
    • 98. Philo J. 1997. New modified Fujita-MacCosham solution for species of molecular weight <10,000. Biophys. J. 72:435-44
    • (1997) Biophys. J. , vol.72 , pp. 435-444
    • Philo, J.1
  • 99
    • 0028077586 scopus 로고
    • Interactions of neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3*BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors
    • 99. Philo J, Talvenheimo J, Wen J, Rosenfeld R, Welcher A, et al. 1994. Interactions of neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3*BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors. J. Biol. Chem. 269:27840-46
    • (1994) J. Biol. Chem. , vol.269 , pp. 27840-27846
    • Philo, J.1    Talvenheimo, J.2    Wen, J.3    Rosenfeld, R.4    Welcher, A.5
  • 101
    • 0022326986 scopus 로고
    • Calculation of partial specific volumes of proteins in 8 M urea solution
    • 101. Prakash V, Timasheff SN. 1985. Calculation of partial specific volumes of proteins in 8 M urea solution. Methods Enzymol. 117:53-60
    • (1985) Methods Enzymol. , vol.117 , pp. 53-60
    • Prakash, V.1    Timasheff, S.N.2
  • 103
    • 0027930961 scopus 로고
    • The concentration dependence of the activity coefficient of the human spectrin heterodimer. A quantitative test of the Adams-Fujita approximation
    • 103. Ralston GB. 1994. The concentration dependence of the activity coefficient of the human spectrin heterodimer. A quantitative test of the Adams-Fujita approximation. Biophys. Chem. 52:51-61
    • (1994) Biophys. Chem. , vol.52 , pp. 51-61
    • Ralston, G.B.1
  • 104
    • 0022293589 scopus 로고
    • Determination of protein molecular weight in complexes with detergent without knowledge of binding
    • 104. Reynolds JA, McCaslin DR. 1985. Determination of protein molecular weight in complexes with detergent without knowledge of binding. Methods Enzymol. 117:41-53
    • (1985) Methods Enzymol. , vol.117 , pp. 41-53
    • Reynolds, J.A.1    McCaslin, D.R.2
  • 105
    • 2142856595 scopus 로고
    • Determination of molecular weight of the protein moiety in protein-detergent complexes without direct knowledge of detergent binding
    • 105. Reynolds JA, Tanford C. 1976. Determination of molecular weight of the protein moiety in protein-detergent complexes without direct knowledge of detergent binding. Proc. Natl. Acad. Sci. USA 73(12):4467-70
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , Issue.12 , pp. 4467-4470
    • Reynolds, J.A.1    Tanford, C.2
  • 107
    • 0027200483 scopus 로고
    • New developments in the study of biomolecular associations via sedimentation equilibrium
    • 107. Rivas GA, Minton AR 1993. New developments in the study of biomolecular associations via sedimentation equilibrium. Trends Biochem. Sci. 18:284-87
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 284-287
    • Rivas, G.A.1    Minton, A.R.2
  • 108
    • 0017107966 scopus 로고
    • Sedimentation equilibrium techniques: Multiple speed analyses and an overspeed procedure
    • 108. Roark DE. 1976. Sedimentation equilibrium techniques: multiple speed analyses and an overspeed procedure. Biophys, Chem. 5:185-96
    • (1976) Biophys, Chem. , vol.5 , pp. 185-196
    • Roark, D.E.1
  • 109
    • 0014667364 scopus 로고
    • Studies of self-associating systems by equilibrium ultracentrifugation
    • 109. Roark DE, Yphantis DA. 1969. Studies of self-associating systems by equilibrium ultracentrifugation. Ann. NY Acad. Sci. 164:245-78
    • (1969) Ann. NY Acad. Sci. , vol.164 , pp. 245-278
    • Roark, D.E.1    Yphantis, D.A.2
  • 110
    • 0015230398 scopus 로고
    • Equilibrium centrifugation of nonideal systems. The Donnan effect in self-associating systems
    • 110. Roark DE, Yphantis DA. 1971. Equilibrium centrifugation of nonideal systems. The Donnan effect in self-associating systems. Biochemistry 10:3241-49
    • (1971) Biochemistry , vol.10 , pp. 3241-3249
    • Roark, D.E.1    Yphantis, D.A.2
  • 112
    • 0022495489 scopus 로고
    • Triton X-100 induced dissociation of beef heart cytochrome c oxidase into monomers
    • 112. Robinson NC, Talbert L. 1986. Triton X-100 induced dissociation of beef heart cytochrome c oxidase into monomers. Biochemistry 25:2328-35
    • (1986) Biochemistry , vol.25 , pp. 2328-2335
    • Robinson, N.C.1    Talbert, L.2
  • 113
    • 0017611984 scopus 로고
    • The concentration dependence of transport processes: A general description applicable to the sedimentation, translational diffusion, and viscosity coefficients of macromolecular solutes
    • 113. Rowe AJ. 1977. The concentration dependence of transport processes: a general description applicable to the sedimentation, translational diffusion, and viscosity coefficients of macromolecular solutes. Biopolymers 16:2595-611
    • (1977) Biopolymers , vol.16 , pp. 2595-2611
    • Rowe, A.J.1
  • 114
    • 0030660412 scopus 로고    scopus 로고
    • Linkage between operator binding and dimer to octamer self-assembly of bacteriophage lambda c1 repressor
    • 114. Rusinova E, Ross JBA, Laue TM, Sowers LC, Senear DF. 1997. Linkage between operator binding and dimer to octamer self-assembly of bacteriophage lambda c1 repressor. Biochemistry 36:12994-3003
    • (1997) Biochemistry , vol.36 , pp. 12994-13003
    • Rusinova, E.1    Ross, J.B.A.2    Laue, T.M.3    Sowers, L.C.4    Senear, D.F.5
  • 116
    • 0027928436 scopus 로고
    • Simultaneous radial and wavelength analysis with the Optima XL-A analytical ultracentrifuge
    • 116. Schuck P 1994. Simultaneous radial and wavelength analysis with the Optima XL-A analytical ultracentrifuge. Prog. Colloid Polym. Sci. 94:1-13
    • (1994) Prog. Colloid Polym. Sci. , vol.94 , pp. 1-13
    • Schuck, P.1
  • 117
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation
    • 117. Schuck P. 1998. Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation. Biophys. J. 75:1503-12
    • (1998) Biophys. J. , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 118
    • 0032524088 scopus 로고    scopus 로고
    • Rapid determination of molar mass in modified Archibald experiments using direct fitting of the Lamm equation
    • 118. Schuck P, Millar DB. 1998. Rapid determination of molar mass in modified Archibald experiments using direct fitting of the Lamm equation. Anal. Biochem. 259:48-53
    • (1998) Anal. Biochem. , vol.259 , pp. 48-53
    • Schuck, P.1    Millar, D.B.2
  • 120
    • 0027278788 scopus 로고
    • The primary self-assembly reaction of bacteriophage lambda cI repressor dimers is to octamer
    • 120. Senear DF, Laue TM, Ross JBA, Waxman E, Eaton SF, et al. 1993. The primary self-assembly reaction of bacteriophage lambda cI repressor dimers is to octamer. Biochemistry 32:6179-89
    • (1993) Biochemistry , vol.32 , pp. 6179-6189
    • Senear, D.F.1    Laue, T.M.2    Ross, J.B.A.3    Waxman, E.4    Eaton, S.F.5
  • 121
    • 0019889068 scopus 로고
    • Effects of saccharide and salt binding on dimertetramer equilibrium of concanavalin A
    • 121. Senear DF, Teller DC. 1981. Effects of saccharide and salt binding on dimertetramer equilibrium of concanavalin A. Biochemistry 20:3083-91
    • (1981) Biochemistry , vol.20 , pp. 3083-3091
    • Senear, D.F.1    Teller, D.C.2
  • 122
    • 0019889057 scopus 로고
    • Thermodynamics of concanavalin A dimer-tetramer self-association: Sedimentation equilibrium studies
    • 122. Senear DF, Teller DC. 1981. Thermodynamics of concanavalin A dimer-tetramer self-association: sedimentation equilibrium studies. Biochemistry 20:3076-83
    • (1981) Biochemistry , vol.20 , pp. 3076-3083
    • Senear, D.F.1    Teller, D.C.2
  • 123
    • 0025700708 scopus 로고
    • Thermodynamic nonideality in macromolecular solutions. Evaluation of parameters for the prediction of covolume effects
    • 123. Shearwin KE, Winzor DJ. 1990. Thermodynamic nonideality in macromolecular solutions. Evaluation of parameters for the prediction of covolume effects. Eur. J. Biochem. 190:523-29
    • (1990) Eur. J. Biochem. , vol.190 , pp. 523-529
    • Shearwin, K.E.1    Winzor, D.J.2
  • 124
    • 0018917327 scopus 로고
    • Graphical analysis of nonideal monomer N-mer, isodesmic and type III indefinite self-associating systems by equilibrium ultracentrifugation
    • 124. Stafford WF. 1980. Graphical analysis of nonideal monomer N-mer, isodesmic and type III indefinite self-associating systems by equilibrium ultracentrifugation. Biophys. J. 29:149-66
    • (1980) Biophys. J. , vol.29 , pp. 149-166
    • Stafford, W.F.1
  • 125
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • 125. Stafford WF. 1992. Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203:295-301
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford, W.F.1
  • 127
    • 0002852793 scopus 로고    scopus 로고
    • Time difference sedimentation velocity analysis of rapidly reversible interacting systems: Determination of equilibrium constants by nonlinear curve filling procedures
    • Abstr.
    • 127. Stafford WF. 1998. Time difference sedimentation velocity analysis of rapidly reversible interacting systems: determination of equilibrium constants by nonlinear curve filling procedures. Biophys. J. 74:A301 (Abstr.)
    • (1998) Biophys. J. , vol.74
    • Stafford, W.F.1
  • 128
    • 0028821154 scopus 로고
    • An optical thermometer for direct measurement of cell temperature in the Beckman Instruments XL-A analytical ultracentrifuge
    • 128. Stafford WF, Liu S. 1995. An optical thermometer for direct measurement of cell temperature in the Beckman Instruments XL-A analytical ultracentrifuge. Anal. Biochem. 224:199-202
    • (1995) Anal. Biochem. , vol.224 , pp. 199-202
    • Stafford, W.F.1    Liu, S.2
  • 130
    • 0017917637 scopus 로고
    • Determination of partial specific-volumes for lipid-associated proteins
    • ed. CHW Hirs, SN Timasheff. New York: Academic
    • 130. Steele JCH Jr, Tanford C, Reynolds JA. 1978. Determination of partial specific-volumes for lipid-associated proteins. In Molecular Weight Determinations, ed. CHW Hirs, SN Timasheff, pp. 11-23. New York: Academic
    • (1978) Molecular Weight Determinations , pp. 11-23
    • Steele J.C.H., Jr.1    Tanford, C.2    Reynolds, J.A.3
  • 132
    • 0016218601 scopus 로고
    • Molecular characterization of proteins in detergent solutions
    • 132. Tanford C, Nozaki Y, Reynolds JA, Makino S. 1974, Molecular characterization of proteins in detergent solutions. Biochemistry 13:11:2369-76
    • (1974) Biochemistry , vol.13 , Issue.11 , pp. 2369-2376
    • Tanford, C.1    Nozaki, Y.2    Reynolds, J.A.3    Makino, S.4
  • 133
    • 0018535196 scopus 로고
    • Calculated molecular weight of proteins in high ionic strengths: Contribution of the apparent isopotential specific volume
    • 133. Tuengler P, Long GL, Durchschlag H. 1979. Calculated molecular weight of proteins in high ionic strengths: contribution of the apparent isopotential specific volume. Anal. Biochem. 98:481-84
    • (1979) Anal. Biochem. , vol.98 , pp. 481-484
    • Tuengler, P.1    Long, G.L.2    Durchschlag, H.3
  • 134
    • 0013575443 scopus 로고
    • Sedimentation
    • Englewood Cliffs, NJ: Prentice Hall
    • 134. Van Holde KE. 1985, Sedimentation. In Physical Biochemistry, pp. 110-36. Englewood Cliffs, NJ: Prentice Hall
    • (1985) Physical Biochemistry , pp. 110-136
    • Van Holde, K.E.1
  • 135
    • 0031647711 scopus 로고    scopus 로고
    • Analytical ultracentrifugation from 1924 to the present: A remarkable history
    • In press
    • 135. Van Holde KE, Hansen JC. 1999. Analytical ultracentrifugation from 1924 to the present: a remarkable history. Chem-Tracts: Biochem. Mol. Biol. 11:In press
    • (1999) Chem-tracts: Biochem. Mol. Biol. , vol.11
    • Van Holde, K.E.1    Hansen, J.C.2
  • 136
    • 0017806223 scopus 로고
    • Boundary analysis of sedimentation-velocity experiments with monodisperse and paucidisperse solutes
    • 136. Van Holde KE, Weischet WO. 1978. Boundary analysis of sedimentation-velocity experiments with monodisperse and paucidisperse solutes. Biopolymers 17:1387-403
    • (1978) Biopolymers , vol.17 , pp. 1387-1403
    • Van Holde, K.E.1    Weischet, W.O.2
  • 137
    • 0017107967 scopus 로고
    • Molecular weights and molecular-weighl distributions from ultracentrifugation of nonideal solutions
    • 137. Wan PJ, Adams ET Jr. 1976. Molecular weights and molecular-weighl distributions from ultracentrifugation of nonideal solutions. Biophys. Chem. 5:207-41
    • (1976) Biophys. Chem. , vol.5 , pp. 207-241
    • Wan, P.J.1    Adams E.T., Jr.2
  • 138
    • 0026736047 scopus 로고
    • Tissue factor and its extracellular soluble domain: The relationship between intermolecular association with factor Vlla and enzymatic activity of the complex
    • 138. Waxman E, Ross JBA, Laue TM, Guha A, Thiruvikraman SV, et al. 1992.Tissue factor and its extracellular soluble domain: the relationship between intermolecular association with factor Vlla and enzymatic activity of the complex. Biochemistry 31:3998 4003
    • (1992) Biochemistry , vol.31 , pp. 3998-4003
    • Waxman, E.1    Ross, J.B.A.2    Laue, T.M.3    Guha, A.4    Thiruvikraman, S.V.5
  • 139
    • 0022358166 scopus 로고
    • Molecular characterization of the human erythrocyte anion transport protein in octyl glucoside
    • 139. Werner PK, Reithmeier RAF. 1985. Molecular characterization of the human erythrocyte anion transport protein in octyl glucoside. Biochemistry 24:6375-81
    • (1985) Biochemistry , vol.24 , pp. 6375-6381
    • Werner, P.K.1    Reithmeier, R.A.F.2
  • 140
    • 0024582234 scopus 로고
    • Boundary spreading in sedimentation velocity experiments on partially liganded aspartate transcarbamoylase
    • 140. Werner WE, Cann JR, Schachman HK. 1989. Boundary spreading in sedimentation velocity experiments on partially liganded aspartate transcarbamoylase. J. Mol. Biol. 206:231-37
    • (1989) J. Mol. Biol. , vol.206 , pp. 231-237
    • Werner, W.E.1    Cann, J.R.2    Schachman, H.K.3
  • 143
    • 0027292011 scopus 로고
    • Thermodynamic nonideality in macromolecular solutions: Interpretation of virial coefficients
    • 143. Wills PR, Comper WD, Winzor DJ. 1993. Thermodynamic nonideality in macromolecular solutions: interpretation of virial coefficients. Arch. Biochem. Biophys. 300:206-211
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 206-211
    • Wills, P.R.1    Comper, W.D.2    Winzor, D.J.3
  • 144
    • 0028883959 scopus 로고
    • Measurement of thermodynamic nonideality arising from volume-exclusion interactions between proteins and polymers
    • 144. Wills PR, Georgalis Y, Dijk J, Winzor DJ. 1995. Measurement of thermodynamic nonideality arising from volume-exclusion interactions between proteins and polymers. Biophys. Chem. 57:37-46
    • (1995) Biophys. Chem. , vol.57 , pp. 37-46
    • Wills, P.R.1    Georgalis, Y.2    Dijk, J.3    Winzor, D.J.4
  • 145
    • 0001639451 scopus 로고
    • Thermodynamic non-ideality and sedimentation equilibrium
    • ed. SE Harding, AJ Rowe, JC Horton. Cambridge, UK: R. Soc. Chem.
    • 145. Wills PR, Winzor DJ. 1992. Thermodynamic non-ideality and sedimentation equilibrium. In Analytical Ultracentrifugation in Biochemistry und Polymer Science, ed. SE Harding, AJ Rowe, JC Horton, pp. 311-30. Cambridge, UK: R. Soc. Chem.
    • (1992) Analytical Ultracentrifugation in Biochemistry und Polymer Science , pp. 311-330
    • Wills, P.R.1    Winzor, D.J.2
  • 147
    • 0028802257 scopus 로고
    • Thermodynamic nonideality of enzyme solutions supplemented with inert solutes: Yeast hexokinase revisited
    • 147. Winzor DJ, Wills PR. 1995. Thermodynamic nonideality of enzyme solutions supplemented with inert solutes: yeast hexokinase revisited. Biophys. Chem. 57:103-10
    • (1995) Biophys. Chem. , vol.57 , pp. 103-110
    • Winzor, D.J.1    Wills, P.R.2
  • 148
    • 0001303393 scopus 로고
    • The viscosity of macromolecules in relation to molecular conformation
    • 148. Yang JT. 1961. The viscosity of macromolecules in relation to molecular conformation. Adv. Protein Chem. 16:323-400
    • (1961) Adv. Protein Chem. , vol.16 , pp. 323-400
    • Yang, J.T.1
  • 149
    • 0000393055 scopus 로고
    • Rapid determination of molecular weights of peptides and proteins
    • 149. Yphantis DA. 1960. Rapid determination of molecular weights of peptides and proteins. Ann. NY Acad. Sci. 88:586-601
    • (1960) Ann. NY Acad. Sci. , vol.88 , pp. 586-601
    • Yphantis, D.A.1
  • 150
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugatiori of dilute solutions
    • 150. Yphantis DA. 1964. Equilibrium ultracentrifugatiori of dilute solutions. Biochemistry 3:297-317
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 151
    • 84912372841 scopus 로고
    • Detection of heterogeneity in self-associating systems
    • ed. N Catsimpoolas. Amsterdam: Elsevier/North Holland Biomed.
    • 151. Yphantis DA, Correia JJ, Johnson ML, Wu G. 1978. Detection of heterogeneity in self-associating systems. In Physical Aspects of Protein Interactions, ed. N Catsimpoolas, pp. 275-303. Amsterdam: Elsevier/North Holland Biomed.
    • (1978) Physical Aspects of Protein Interactions , pp. 275-303
    • Yphantis, D.A.1    Correia, J.J.2    Johnson, M.L.3    Wu, G.4
  • 152
    • 0015386141 scopus 로고
    • Equilibrium centrifugation of nonideal systems. Molecular weight moments for removing the effects of nonideality
    • 152. Yphantis DA, Roark DE. 1972. Equilibrium centrifugation of nonideal systems. Molecular weight moments for removing the effects of nonideality. Biochemistry 11:2925-34
    • (1972) Biochemistry , vol.11 , pp. 2925-2934
    • Yphantis, D.A.1    Roark, D.E.2
  • 153
    • 33947476873 scopus 로고
    • Ultracentifugal characterization by direct measurement of activity. I. Theoretical
    • 153. Yphantis DA, Waugh DF. 1956. Ultracentifugal characterization by direct measurement of activity. I. Theoretical. J. Phys. Chem. 60:623-35
    • (1956) J. Phys. Chem. , vol.60 , pp. 623-635
    • Yphantis, D.A.1    Waugh, D.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.