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  • 1
    Electronic Resource
    Electronic Resource
    A new approach to analytical density gradient equilibrium centrifugation. Simultaneous determination of molecular weight, specific volume, and preferential hydration of human transferrin (1977)
    New York : Wiley-Blackwell
    Journal of Polymer Science: Polymer Physics Edition 15 (1977), S. 733-748 
    Details
    ISSN: 0098-1273
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Human transferrin was examined by analytical density gradient equilibrium centrifugation using a short liquid column and employing an iodinated organic gradient salt. Favorable conditions of low pressure and relatively low ionic strength could therefore be obtained. The short liquid column also permitted the layering of extra salt solution above the protein solution in a liquid equalization stage of each experiment. In this stage the amount of preferentially bound water was determined by measurement of solvation arising from the dissolution of the protein which had been added to the centrifuge cell as freeze-dried material. Since schlieren optics were employed, the refractive index of the macromolecular component in the mixed solution had to be known. This quantity was determined from the refractive index difference of the solvent/solution boundary at the liquid equalization stage of each experiment or, alternatively, by regression analysis of the equilibrium data. The new regression method yielded an anhydrous molecular weight of 78,000 daltons which is the same as the value obtained by the classical density gradient equilibrium method performed under the same conditions. Control experiments showed that the analytical ultracentrifuge cell cannot be regarded as a closed, inert system.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1977.180150413
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  • 2
    Electronic Resource
    Electronic Resource
    Concentrated protein solutions in the analytical ultracentrifuge (1980)
    New York : Wiley-Blackwell
    Journal of Polymer Science: Polymer Physics Edition 18 (1980), S. 1963-1978 
    Details
    ISSN: 0098-1273
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Concentrated solutions of transferrin, albumin, immunoglobulin, chymotrypsinogen, transfer-RNA, dextran, and polystyrene were pelleted in the analytical ultracentrifuge. The proteins developed a solvent/pellet boundary which was chracterized at equilibrium by an asymmetric schlieren peak with a “shoulder”. The schlieren curve was at the same level inside the protein pellet as in the solvent above the pellet, indicating that the protein molecules had been packed homogeneously. The protein concentration in the pellet ranged from 0.6 to 0.7 g/ml. Immediately after deceleration was begun, the “shoulder” of the pellet boundary changed into a very sharp peak, leading to a boundary composed of two schlieren peaks. Sedimentation rates were measured for transferrin solutions at concentrations up to 0.3 g/ml.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1980.180180909
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    Paper (German National Licenses)
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