Abstract
There are in general two kinds of articles which have to do with sedimentation behavior. In the one the subject matter is descriptive of the theory and practice of the use of the ultracentrifuge in analysis; in the other consideration is given to the application of the methods so provided in the solution of problems in biology and medicine. This time the author has felt that an attempt to review some selected topics, both as to the main outlines of the theory and the applications of the technique, might be of interest. Because of limitations of space it could not be a balanced, objective account of the subject, so that of choice we have written principally about those aspects of the subject in which we are currently interested and supposedly better informed.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Akeley, D. F. and L. J. Gosting: Studies of the Diffusion of Mixed Solutes with the Gouy Diffusiometer. J. Amer. Chem. Soc. 75, 5685 (1953).
Alberty, R. A. and H. H. Marvin, Jr.: Protein-Ion Interaction by the Moving Boundary Method. Theory of the Method. J. Physic. Coll. Chem. 54, 47 (1950).
Anfinsen, C. B., R. R. Redfield, W. L. Choate, J. Page and W. R. Carroll: Studies on the Gross Structure, Cross-Linkages, and Terminal Sequences in Ribonuclease. J. Biol. Chem. 207, 201 (1954).
Archibald, W. J.: The Process of Diffusion in a Centrifugal Field of Force. Physic. Rev. 53, 746 (1938).
Archibald, W. J.: The Process of Diffusion in a Centrifugal Field of Force. II. Physic. Rev. 54, 371 (1938).
Aschaffenburg, R. and J. Drewry: Occurrence of Different β-Lactoglobulins in Cow Milk. Nature (London) 176, 218 (1955).
Baldwin, R. L.: The Neurotoxin of Shigella Shigae. II. Examination of the Toxin in the Oil-Turbine Ultracentrifuge. Brit. J. exp. Pathol. 34, 217 (1953).
Baldwin, R. L.: Boundary Spreading in Sedimentation Velocity Experiments. II. The Correction of Sedimentation Coefficient Distributions for the Dependence of Sedimentation Coefficient on Concentration. J. Amer. Chem. Soc. 76, 402 (1954).
Baldwin, R. L.: Boundary Spreading in Sedimentation Velocity Experiments. III. Effects of Diffusion on the Measurement of Heterogeneity when Concentration Dependence is Absent. J. Physic. Chem. 58, 1081 (1954).
Baldwin, R. L.: Boundary Spreading in Sedimentation Velocity Experiments. 5. Measurement of the Diffusion Coefficient of Bovine Albumin by Fujita’s Equation. Biochemic. J. 65, 503 (1957).
Baldwin, R. L.: Molecular Weights from Studies of Sedimentation and Diffusion in Three-Component Systems. J. Amer. Chem. Soc. 80, 496 (1958).
Baldwin, R. L.: Equilibrium Sedimentation in a Density Gradient of Materials Having a Continuous Distribution of Effective Densities. Proc. Nat. Acad. Sci. (USA) 45, 939 (1959).
Baldwin, R. L.: Boundary Spreading in Sedimentation Velocity Experiments. VI. A Better Method for Finding Distributions of Sedimentation Coefficient when the Effects of Diffusion are Large. J. Physic. Chem. 63, 1570 (1959).
Baldwin, R. L., L. J. Gosting, J. W. Williams and R. A. Alberty: Transport Processes and the Heterogeneity of Proteins. Discuss. Faraday Soc. 20, 13 (1955).
Baldwin, R. L. and A. G. Ogston: The Diffusion and Sedimentation Coefficients of a Liquid Two-Component System in Terms of Macroscopic Properties of the System. Trans. Faraday Soc. 50, 749 (1954).
Baldwin, R. L. and J. W. Williams: Boundary Spreading in Sedimentation Velocity Experiments. J. Amer. Chem. Soc. 72, 4325 (1950).
Banovitz, J., S. J. Singer and H. R. Wolfe: Precipitin Production in Chickens. XVIII. Physical Chemical Studies on Complexes of Bovine Serum Albumin and its Chicken Antibodies. J. Immunology 82, 481 (1959).
Bell, D. J., H. Gutfreund, R. Cecil and A. G. Ogston: Physicochemical Observations of Some Glycogens. Biochemie. J. 42, 405 (1948).
Boedtker, H. and P. Doty: On the Nature of the Structural Element of Collagen. J. Amer. Chem. Soc. 77, 248 (1955).
Boedtker, H. and P. Doty: The Native and Denatured States of Soluble Collagen. J. Amer. Chem. Soc. 78, 4267 (1956).
Bridgman, W. B.: Some Physical Chemical Characteristics of Glycogen. J. Amer. Chem. Soc. 64, 2349 (1942).
Bridgman, W. B. and J. W. Williams: Optical Problems of the Ultracentrifuge. Ann. New York Acad. Sci. 43, 195 (1942).
Brown, R. A. and S. N. Timasheff: Applications of Moving Boundary Electrophoresis to Protein Systems. In: M. Bier, Electrophoresis. Theory, Methods, and Applications, p. 317. New York and London: Academic Press. 1959.
Butler, J. A. V., D. J. R. Laurence, A. B. Robins and K. V. Shooter: Molecular Weights and Physical Properties of Deoxyribonucleic Acid. Nature (London) 180, 1340 (1957).
Butler, J. A. V., D. M. Phillips and K. V. Shooter: Influence of Protein Heterogeneity of Deoxyribonucleic Acid (DNA). Arch. Biochem. Biophys. 71, 423 (1957).
Buzzell, J. G. and C. Tanford: The Effect of Charge and Ionic Strength on the Viscosity of Ribonuclease. J. Physic. Chem. 60, 1204 (1956).
Cann, J. R., J. G. Kirkwood and R. A. Brown: Theory of Isomerization Equilibrium in Electrophoresis. I. Arch. Biochem. Biophys. 72, 37 (1957).
Cecil, R. and A. G. Ogston: The Accuracy of the Svedberg Oil-Turbine Ultracentrifuge. Biochemic. J. 43, 592 (1948).
Cecil, R. and A. G. Ogston: The Sedimentation Constant, Diffusion Constant and Molecular Weight of Lactoglobulin. Biochemie. J. 44, 33 (1949).
Charlwood, P. A.: Partial Specific Volumes of Proteins in Relation to Composition and Environment. J. Amer. Chem. Soc. 79, 776 (1957).
Creeth, J. M.: Studies of Free Diffusion in Liquids with the Rayleigh Method. III. The Analysis of Known Mixtures and Some Preliminary Investigations with Proteins. J. Physic. Chem. 62, 66 (1958).
Crick, F. H. C. and J. D. Watson: The Complementary Structure of Deoxyribonucleic Acid (DNA). Proc. Roy. Soc. (London) A 223, 80 (1954).
Davison, P. F.: The Effect of Hydrodynamic Shear on the Deoxyribonucleic Acid from T2 and T4 Bacteriophages. Proc. Nat. Acad. Sci. (USA) 45, 1560 (1959).
Dayhoff, M. O., G. E. Perlmann and D. A. MacInnes: The Partial Specific Volumes, in Aqueous Solution, of Three Proteins. J. Amer. Chem. Soc. 74, 2515 (1952).
de Groot, S. R., P. Mazur and J. T. G. Overbeek: Nonequilibrium Thermodynamics of the Sedimentation Potential and Electrophoresis. J. Chem. Physics 20, 1825 (1952).
de Lalla, O. F. and J. W. Gofman: Ultracentrifugal Analysis of Serum Lipoproteins. In: D. Glick, Methods of Biochemical Analysis, Vol. 1, p. 459. New York: Interscience Publ., Inc. 1954.
Doty, P., B. B. McGill and S. A. Rice: The Properties of Sonic Fragments of Deoxyribose Nucleic Acid. Proc. Nat. Acad. Sci. (USA) 44, 432 (1958).
Duclaux, J.: Centrifuges et ultracentrifuges. Traité de Chimie Physique, No. 1228. Paris: Hermann et Cie. 1955.
Edsall, J. T.: The Size, Shape and Hydration of Protein Molecules. In: H. Neurath and K. Bailey, The Proteins, Vol. I, Part B, p. 549. New York: Academic Press. 1953.
Edsall, J. T.: Aspects actuels de la biochimie des acides aminés et des protéines. Actualités Biochimiques, No. 20. Paris: Masson et Cie. 1958.
Eriksson, A. F. V.: Mass Distribution of Unfractionated and Fractionated Polymethyl Methacrylates Determined by Ultracentrifugation and Fractional Precipitation. Acta Chem. Scand. 10, 360 (1956).
Faxen, H.: Über eine Differentialgleichung aus der physikalischen Chemie. Ark. Mat. Astron. Fysik 21 B, Nr. 3 (1929).
Field, E. O. and A. G. Ogston: Boundary Spreading in the Migration of a Solute in Rapid Dissociation Equilibrium. Theory and its Application to the Case of Human Hemoglobin. Biochemic. J. 60, 661 (1955).
Flory, P. J.: Principles of Polymer Chemistry. Ithaca: Cornell Univ. Press. 1953.
Fujita, H.: Effects of a Concentration Dependence of the Sedimentation Coefficient in Velocity Ultracentrifugation. J. Chem. Physics 24, 1084 (1956).
Fujita, H.: Evaluation of Diffusion Coefficients from Sedimentation Velocity Measurements. J. Physic. Chem. 63, 1092 (1959).
Gilbert, G. A.: General Discussion. Discuss. Faraday Soc. 20, 68 (1955).
Gilbert, G. A.: Sedimentation and Electrophoresis of Interacting Substances. I. Idealized Boundary Shape for a Single Substance Aggregating Reversibly. Proc. Roy. Soc. (London) A 250, 377 (1959).
Gilbert, G. A. and R. C. L. Jenkins: Boundary Problems in the Sedimentation and Electrophoresis of Complex Systems in Rapid Reversible Equilibrium. Nature (London) 177, 853 (1956).
Gilbert, G. A. and R. C. L. Jenkins: Sedimentation and Electrophoresis Interacting Systems. II. Proc. Roy. Soc. (London) A 253, 420 (1959).
Gofman, J. W.: What We Do Know about Heart Attacks. New York: G. P. Putnam’s Sons. 1958.
Gofman, J. W., M. A. Lauffer, I. H. Page, F. J. Stare, et al.: Evaluation of Serum Lipoprotein and Cholesterol Measurements as Predictors of Clinical Complications of Atherosclerosis. Circulation 14, 691 (1956).
Goldberg, R. J.: A Theory of Antibody-Antigen Reactions. I. Theory for Reactions of Multivalent Antigen with Bivalent and Univalent Antibody. J. Amer. Chem. Soc. 74, 5715 (1952).
Goldberg, R. J.: Sedimentation in the Ultracentrifuge. J. Physic. Chem. 57, 194 (1953).
Goldberg, R. J. and J. W. Williams: Antigen-Antibody Reactions in Theory and Practice. Discuss. Faraday Soc. 13, 224 (1953).
Gosting, L. J.: Solution of Boundary Spreading Equations for Electrophoresis and the Velocity Ultracentrifuge. J. Amer. Chem. Soc. 74, 1548 (1952).
Gosting, L. J.: Measurement and Interpretation of Diffusion Coefficients of Proteins. Adv. Protein Chem. 11, 429 (1956).
Harrington, W. F., P. Johnson and R. H. Ottewill: Bovine Serum Albumin and its Behavior in Acid Solution. Biochemic. J. 62, 569 (1956).
Harrington, W. F. and J. A. Schellman: Evidence for the Instability of Hydrogen-Bonded Peptide Structures in Water, Based on Studies of Ribo-nuclease and Oxidized Ribonuclease. C. R. Trav. Lab. Carlsberg, Sér. chim. 30, 21 (1956).
Heidelberger, M. and K. O. Pedersen: Molecular Weight of Antibodies. J. exp. Medicine 65, 393 (1937).
Herzog, R. O., R. Illig und H. Kudar: Über die Diffusion in molekulardispersen Lösungen. Z. physik. Chem. A 167, 329 (1934).
Hirs, C. H. W., W. H. Stein and S. Moore: Peptides Obtained by Chymotryptic Hydrolysis of Performic Acid-Oxidized Ribonuclease. A Partial Structural Formula for the Oxidized Protein. J. Biol. Chem. 221, 151 (1956).
Hooyman, G. J.: Thermodynamics in Sedimentation of Paucidisperse Systems. Physica 22, 761 (1956).
Hooyman, G. J., H. Holtan, Jr., P. Mazur and S. R. de Groot: Thermodynamics of Irreversible Processes in Rotating Systems. Physica 19, 1095 (1953).
Johnson, J. S., K. A. Kraus and G. Scatchard: Distribution of Charged Polymers at Equilibrium in a Centrifugal Field. J. Physic. Chem. 58, 1034 (1954).
Johnston, J. P. and A. G. Ogston: A Boundary Anomaly Found in the Ultracentrifugal Sedimentation of Mixtures. Trans. Faraday Soc. 42, 789 (1946).
Jullander, I.: Studies on Nitrocellulose Including the Construction of an Osmotic Balance. Ark. Kemi, Mineral. Geol. 21 A, No. 8 (1945).
Kegeles, G. and F. J. Gutter: The Determination of Sedimentation Constants from Fresnel Diffraction Patterns. J. Amer. Chem. Soc. 73, 3770 (1951).
Kinell, P. O. and B. G. Ranby: Ultracentrifugal Sedimentation of Polymolecular Substances. Adv. Colloid Sci. 3, 161 (1950).
Kraemer, E. O.: In: T. Svedberg and K. O. Pedersen, The Ultracentrifuge, p. 327. Oxford: Clarendon Press. 1940.
Lamm, O.: Messung und Berechnung von Sedimentations-gleichgewichten an hochmolekularen Metaphosphaten. Ark. Kemi, Mineral. Geol. 17 A, No. 25 (1944).
Lansing, W. D. and E. O. Kraemer: Molecular Weight Analysis of Mixtures by Sedimentation. J. Amer. Chem. Soc. 57, 1369 (1935).
Lansing, W. D. and E. O. Kraemer: Solvation and the Determination of Molecular Weights by Means of the Svedberg Ultracentrifuge. J. Amer. Chem. Soc. 58, 1471 (1936).
Larner, J., B. R. Ray and H. F. Crandall: Pattern of Action of Crystalline Muscle Phosphorylase on Glycogen as Determined from Molecular Size Distribution Studies. J. Amer. Chem. Soc. 78, 5890 (1956).
Lauffer, M. A. and I. J. Bendet: The Hydration of Viruses. Adv. Virus Research 2, 241 (1954).
Levinthal, C.: The Mechanism of DNA Replication and Genetic Recombination in Phage. Proc. Nat. Acad. Sci. (USA) 42, 394 (1956).
Linderström-Lang, K. U.: Structure and Enzymatic Breakdown of Proteins. Cold Spring Harbor Sympos. Quant. Biol. 14, 117 (1950).
Linderström-Lang, K. U.: Proteins and Enzymes. Stanford Univ. Publ., Univ. Ser., Med. Sci., Lane Medical Lectures, Vol. VI, 1952.
Lindgren, F. T., H. A. Elliott and J. W. Gofman: The Ultracentrifugal Characterization and Isolation of Human Blood Lipids and Lipoproteins, with Applications to the Study of Atherosclerosis. J. Physic. Coll. Chem. 55, 80 (1951).
Loeb, G. I. and H. A. Scheraga: Hydrodynamic and Thermodynamic Properties of Bovine Serum Albumin at Low pH. J. Physic. Chem. 60, 1633 (1956).
Longsworth, L. G.: National Academy of Sciences Conference on the Ultra-centrifuge. Proc. Nat. Acad. Sci. (USA) 36, 502 (1950).
Longsworth, L. G.: Temperature Dependence of Diffusion in Aqueous Solutions. J. Physic. Chem. 58, 770 (1954).
Longsworth, L. G.: Moving Boundary Electrophoresis—Theory. In: M. Bier, Electrophoresis. Theory, Methods, and Applications, p. 91. New York and London: Academic Press. 1959.
Longsworth, L. G. and C. F. Jacobsen: An Electrophoretic Study of the Binding of Salt Ions by β-Lactoglobulin and Bovine Serum Albumin. J. Physic. Coll. Chem. 53, 126 (1949).
Lundgren, H. P. and W. H. Ward: Molecular Size of Proteins. In: D. M. Greenberg, Amino Acids and Proteins, p. 312. Springfield: Charles C. Thomas. 1951.
Madsen, N. B. and C. F. Cori: The Binding of Glycogen and Phosphorylase. J. Biol. Chem. 233, 1251 (1958).
Makinodan, T., N. Gengozian and R. E. Canning: Demonstration of a Normal Serum Microglobulin Coprecipitating with the Bovine Serum Albumin (BSA)-Chicken Anti-BSA Aggregate. Science (Washington) 130, 1419 (1959).
Mandelkern, L. and P. J. Flory: The Frictional Coefficient for Flexible Chain Molecules in Dilute Solution. J. Chem. Physics 20, 212 (1952).
Mandelkern, L., W. R. Krigbaum, H. A. Scheraga and P. J. Flory: Sedimentation Behavior of Flexible Chain Molecules: Polyisobutylene. J. Chem. Physics 20, 1392 (1952).
Marrack, J. R., H. Hoch and R. G. S. Johns: The Valency of Antibodies. Brit. J. exp. Pathol. 32, 212 (1951).
Massey, V., W. F. Harrington and B. S. Hartley: Physical Properties of Chymotrypsin and Chymotrypsinogen Using the Depolarization of Fluorescence Technique. Discuss. Faraday Soc. 20, 24 (1955).
McBain, J. W.: The Determination of Bound Water by Means of the Ultra-centrifuge. J. Amer. Chem. Soc. 58, 315 (1936).
McMeekin, T. L. and K. Marshall: Specific Volumes of Proteins and the Relationship to their Amino Acid Contents. Science (Washington) 116, 142 (1952).
Meselson, M. and F. W. Stahl: The Replication of DNA in Escherichia Coli. Proc. Nat. Acad. Sci. (USA) 44, 671 (1958).
Meselson, M., F. W. Stahl and J. Vinograd: Equilibrium Sedimentation of Macromolecules in Density Gradients. Proc. Nat. Acad. Sci. (USA) 43, 581 (1957).
Miller, L. E. and F. A. Hamm: Macromolecular Properties of Polyvinylpyrrolidone: Molecular Weight Distribution. J. Physic. Chem. 57, 110 (1953).
Moody, L. S.: II. The Molecular Behavior of Insulin in Acid Solution. Dissert., University of Wisconsin, 1944.
Neurath, H. and W. J. Dreyer: Mechanism of Activation of Trypsinogen and Chymotrypsinogen. Discuss. Faraday Soc. 20, 32 (1955).
Nichols, J. B. and E. D. Bailey: Determinations with the Ultracentrifuge. In: A. Weissberger, Physical Methods of Organic Chemistry, 2nd ed., p. 621. New York: Interscience Publ. Inc. 1949.
Nishihara, T. and P. Doty: The Sonic Fragmentation of Collagen Macro-molecules. Proc. Nat. Acad. Sci. (USA) 44, 411 (1958).
O’Donnell, I. J., R. L. Baldwin and J. W. Williams: Correlation of the N ⇋α Reaction of Thyroglobulin with the Type of Breakdown Produced by Papain. Biochim. Biophys. Acta 28, 294 (1958).
O’Donnell, I. J. and L. J. Gosting: The Concentration Dependence of the Four Diffusion Coefficients of the System NaCl-KCl-H2O at 25° C. In: W. J. Hamer, The Structure of Electrolytic Solutions, p. 160. New York: J. Wiley and Sons, Inc. 1959.
Ogston, A. G.: Dimensions of Solute Particles from Dynamic Properties of their Solutions. Trans. Faraday Soc. 49, 1481 (1953).
Ogston, A. G. and J. M. A. Tilley: Studies on the Heterogeneity of Crystallized β-Lactoglobulin. Biochemic. J. 59, 644 (1955).
Ogston, A. G. and M. P. Tombs: Heterogeneity of Bovine β-Lactoglobulin. Biochemic. J. 66, 399 (1957).
Ogston, A. G. and E. F. Woods: Sedimentation of Some Fractions of Degraded Dextran. Trans. Faraday Soc. 50, 635 (1954).
Oncle y, J. L.: private communication.
Oncley, J. L., E. Ellenbogen, D. Gitlin and F. R. N. Gurt: Protein-Protein Interactions. J. Physic. Chem. 56, 85 (1952).
Oncley, J. L., K. W. Walton and D. G. Cornwell: A Rapid Method for the Bulk Isolation of β-Lipoproteins from Human Plasma. J. Amer. Chem. Soc. 79, 4666 (1957).
Pappenheimer, A. M., Jr., H. P. Lundgren and J. W. Williams: Studies on the Molecular Weight of Diphtheria Toxin, Antitoxin, and their Reaction Products. J. exp. Medicine 71, 247 (1940).
Pedersen, K. O.: Über das Sedimentationsgleichgewicht von anorganischen Salzen in der Ultrazentrifuge. Z. physik. Chem. A 170, 41 (1934).
Pedersen, K. O.: Ultracentrifugal and Electrophoretic Studies on the Milk Proteins. II. The Lactoglobulin of Palmer. Biochemic. J. 30, 961 (1936).
Pedersen, K. O.: On Charge and Specific Ion Effects on Sedimentation in the Ultracentrifuge. J. Physic. Chem. 62, 1282 (1958).
Peller, L.: Sedimentation in Multicomponent Systems. J. Chem. Physics 29, 415 (1958).
Perrin, F.: Mouvement brownien d’un ellipsoïde. II. Rotation libre et dépolarisation des fluorescences. Translation et diffusion de molécules ellipsoïdales. J. phys., Radium [7] 7, 1 (1936).
Polglase, W. J., D. M. Brown and E. L. Smith: Studies on Human Glycogen. II. Sedimentation in the Ultracentrifuge. J. Biol. Chem. 199, 105 (1952).
Reichmann, M. E., S. A. Rice, C. A. Thomas and P. Doty: Further Examination of the Molecular Weight and Size of Desoxypentose Nucleic Acid. J. Amer. Chem. Soc. 76, 3047 (1954).
Rich, A. and F. H. C. Crick: Structure of Collagen. Nature (London) 176, 915 (1955).
Rolfe, R. and M. Meselson: The Relative Homogeneity of Microbial DNA. Proc. Nat. Acad. Sci. (USA) 45, 1039 (1959).
Rosenkranz, H. S. and A. Bendich: Sedimentation Studies of Fractions of Deoxyribonucleic Acid. J. Amer. Chem. Soc. 81, 902 (1959).
Rosenkranz, H. S. and A. Bendich: Studies on the Sedimentation Behavior of Artificial Mixtures of Deoxyribonucleic Acid. J. Amer. Chem. Soc. 81, 2842 (1959).
Rosenkranz, H. S. and A. Bendich: Studies on the Effect of Heat on Deoxyribonucleic Acid. J. Amer. Chem. Soc. 81, 6255 (1959).
Rothen, A.: Molecular Weight and Electrophoresis of Crystalline Ribonuclease. J. Gen. Physiol. 24, 203 (1940).
Sadron, C.: Methods of Determining the Form and Dimensions of Particles in Solution: a Critical Survey. Progr. Biophys. Biophys. Chem. 3, 237 (1953).
Schachman, H. K.: Ultracentrifugation in Biochemistry. New York and London: Academic Press. 1959.
Schachman, H. K. and M. A. Lauffer: The Hydration, Size and Shape of Tobacco Mosaic Virus. J. Amer. Chem. Soc. 71, 536 (1949).
Schachman, H. K. and M. A. Lauffer: The Density Correction of Sedimentation Constants. J. Amer. Chem. Soc. 72, 4266 (1950).
Scheraga, H. A. and L. Mandelkern: Consideration of the Hydrodynamic Properties of Proteins. J. Amer. Chem. Soc. 75, 179 (1953).
Schumaker, V. N. and H. K. Schachman: Ultracentrifugal Analysis of Dilute Solutions. Biochim. Biophys. Acta 23, 628 (1957).
Shooter, K. V. and J. A. V. Butler: Sedimentation of Deoxyribonucleic Acid at Low Concentrations. Trans. Faraday Soc. 52, 734 (1956).
Signer, R. and H. Gross: Ultrazentrifugale Polydispersitätsbestimmungen an hochpolymeren Stoffen. 95. Mitt, über hochpolymere Verbindungen. Helv. Chim. Acta 17, 726 (1934).
Singer, S. J. and D. H. Campbell: Physical Chemical Studies of Soluble Antigen-Antibody Complexes. I. The Valence of Precipitating Rabbit Antibody. J. Amer. Chem. Soc. 74, 1794 (1952).
Singer, S. J. and D. H. Campbell: Physical Chemical Studies of Soluble Antigen-Antibody Complexes. II. Equilibrium Properties. J. Amer. Chem. Soc. 75, 5577 (1953).
Singer, S. J. and D. H. Campbell: Physical Chemical Studies of Soluble Antigen-Antibody Complexes. III. Thermodynamics of the Reaction between Bovine Serum Albumin and its Rabbit Antibodies. J. Amer. Chem. Soc. 77, 3499 (1955).
Singer, S. J. and D. H. Campbell: Physical Chemical Studies of Soluble Antigen-Antibody Complexes. IV. The Effect of pH on the Reaction between Bovine Serum Albumin and its Rabbit Antibodies. J. Amer. Chem. Soc. 77, 3504 (1955).
Singer, S. J. and D. H. Campbell: Physical Chemical Studies of Soluble Antigen-Antibody Complexes. V. Thermodynamics of the Reaction between Ovalbumin and its Rabbit Antibodies. J. Amer. Chem. Soc. 77, 4851 (1955).
Singer, S. J., L. Eggman and D. H. Campbell: Physical Chemical Studies of Soluble Antigen-Antibody Complexes. VI. The Effect of pH on the Reaction between Ovalbumin and its Rabbit Antibodies. J. Amer. Chem. Soc. 77, 4855 (1955).
Smith, R. F. and D. R. Briggs: Electrophoretic Analysis of Protein Interaction. I. Interaction of Bovine Serum Albumin and Methyl Orange. J. Physic. Coll. Chem. 54, 33 (1950).
Smithies, O.: The Application of Four Methods for Assessing Protein Homogeneity to Crystalline β-Lactoglobulin: an Anomaly in Phase Rule Solubility Tests. Biochemic. J. 58, 31 (1954).
Steiner, R. F.: Reversible Association Processes of Globular Proteins. V. The Study of Associating Systems by the Methods of Macromolecular Physics. Arch. Biochem. Biophys. 49, 400 (1954).
Sueoka, N.: A Statistical Analysis of Deoxyribonucleic Acid Distribution in Density Gradient Centrifugation. Proc. Nat. Acad. Sci. (USA) 45, 1480 (1959).
Sueoka, N., J. Marmur and P. Doty: Heterogeneity of Deoxyribonucleic Acids. II. Dependence of the Density of Deoxyribonucleic Acids on Guanine-Cytosine Content. Nature (London) 183, 1429 (1959).
Svedberg, T.: Zentrifugierung, Diffusion und Sedimentationsgleichgewicht von Kolloiden und hochmolekularen Stoffen. Kolloid-Z. 36, Erg.-Bd., 53 (1925).
Svedberg, T. and J. B. Nichols: Determination of Size and Distribution of Size of Particle by Centrifugal Methods. J. Amer. Chem. Soc. 45, 2910 (1923).
Svedberg, T. and K. O. Pedersen: The Ultracentrifuge. Oxford: Clarendon Press. 1940.
Svedberg, T. and H. Rinde: Determination of the Distribution of Size of Particles in Disperse Systems. J. Amer. Chem. Soc. 45, 943 (1923).
Svedberg, T. and H. Rinde: The Ultra-centrifuge, a New Instrument for the Determination of Size and Distribution of Size of Particle in Amicroscopic Colloids. J. Amer. Chem. Soc. 46, 2677 (1924).
Taylor, J. H., P. S. Woods and W. L. Hughes: The Organization and Duplication of Chromosomes as Revealed by Autoradiographic Studies Using Tritium-Labeled Thymidine. Proc. Nat. Acad. Sci. (USA) 43, 122 (1957).
Timasheff, S. N. and J. G. Kirkwood: Electrophoresis-Convection Applied to the Complexed Insulin-Protamine System. J. Amer. Chem. Soc. 75, 3124 (1953).
Timasheff, S. N. and R. Townend: The Association Behavior of β-Lacto-globulins A and B. J. Amer. Chem. Soc. 80, 4433 (1958).
Tiselius, A.: Über die Berechnung thermodynamischer Eigenschaften von kolloiden Lösungen aus Messungen mit der Ultrazentrifuge. Z. physik. Chem. 124, 449 (1926).
Tiselius, A.: Study of the Electrophoresis of Proteins by the Moving-Boundary Method. Nova Acta Regiae Soc. Sci. Upsaliensis 7, No. 4 (1930).
Tiselius, A.: Über den Einfluß der Ladung auf die Sedimentationsgeschwindigkeit von Kolloiden, besonders in der Ultrazentrifuge. Kolloid-Z. 59, 306 (1932).
Townend, R. and S. N. Timasheff: The pH Dependence of the Association of β-Lactoglobulin. Arch. Biochem. Biophys. 63, 482 (1956).
Townend, R. and S. N. Timasheff: The Molecular Weight of β-Lactoglobulin. J. Amer. Chem. Soc. 79, 3613 (1957).
Trautman, R., V. N. Schumaker, W. F. Harrington and H. K. Schachman: The Determination of Concentrations in the Ultracentrifugation of Two-Component Systems. J. Chem. Physics 22, 555 (1954).
Van Holde, K. E. and R. L. Baldwin: Rapid Attainment of Sedimentation Equilibrium. J. Physic. Chem. 62, 734 (1958).
Wales, M. and J. W. Williams: Effect of Solvation on Sedimentation Experiments. J. Polymer Sci. 8, 449 (1952).
Williams, J. W.: Sedimentation Analysis and Some Related Problems. J. Polymer Sci. 12, 351 (1954).
Williams, J. W., R. L. Baldwin, W. M. Saunders and P. G. Squire: Boundary Spreading in Sedimentation Velocity Experiments. I. The Enzymatic Degradation of Serum Globulins. J. Amer. Chem. Soc. 74, 1542 (1952).
Williams, J. W. and W. M. Saunders: Size Distribution Analysis in Plasma Extender Systems. II. Dextran. J. Physic. Chem. 58, 854 (1954).
Williams, J. W., W. M. Saunders and J. S. Cicirelli: Size Distribution Analysis in Plasma Extender Systems. I. Gelatin. J. Physic. Chem. 58, 774 (1954).
Williams, J. W., K. E. Van Holde, R. L. Baldwin and H. Fujita: The Theory of Sedimentation Analysis. Chem. Rev. 58, 715 (1958).
Yeandle, S.: Effect of Electric Field on Equilibrium Sedimentation of Macromolecules in a Density Gradient of Cesium Chloride. Proc. Nat. Acad. Sci. (USA) 45, 184 (1959).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1960 Springer-Verlag in Vienna
About this chapter
Cite this chapter
Williams, J.W. (1960). Selected Subjects in Sedimentation Analysis, with Some Applications to Biochemistry. In: Zechmeister, L. (eds) Fortschritte der Chemie organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products / Progrés Dans la Chimie des Substances Organiques Naturelles. Fortschritte der Chemie organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products / Progrés Dans la Chimie des Substances Organiques Naturelles, vol 18. Springer, Vienna. https://doi.org/10.1007/978-3-7091-7159-2_8
Download citation
DOI: https://doi.org/10.1007/978-3-7091-7159-2_8
Publisher Name: Springer, Vienna
Print ISBN: 978-3-7091-7161-5
Online ISBN: 978-3-7091-7159-2
eBook Packages: Springer Book Archive