Abstract
By means of the Svedberg high-speed ultra-centrifuge it is possible to analyse mixtures of different molecular species, since the sedimentation involves a partial separation of the different sizes present. The concentration of the components may therefore be calculated from the sedimentation diagram. But during the study of protein mixtures in the ultra-centrifuge it has often been observed that the concentration of the different sedimenting molecules thus calculated were not the same as those determined analytically. Generally the apparent concentration of the faster sedimenting molecule was smaller, when calculated from the sedimentation diagram, whereas it was higher for the slower sedimenting molecule. McFarlane1, who first studied the problem on some artificial serum mixtures, thought that the effect was due to some specific interaction between the albumin and the globulin. Later, R. A. Kekwick and I studied some mixtures of serum-albumin and lactoglobulin. In this case serum-albumin, the faster sedimenting molecule, is found in too low concentration, and the lactoglobulin is found in too high concentration. From these experiments I concluded that the phenomenon was caused by some medium effect produced by the slower sedimenting protein molecules on the faster sedimenting ones, and that the effect was due to a real dissociation of the faster sedimenting molecules. If this is true, one would expect that it would be possible to produce the effect by means of lower molecular substances related to proteins, such as amino acids, polypeptides and protamines.
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See, for example, A. S. McFarlane : Biochem. J., 29, 407 (1935).
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PEDERSEN, K. Molecular State of Proteins in Mixtures and Concentrated Solutions. Nature 138, 363 (1936). https://doi.org/10.1038/138363a0
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DOI: https://doi.org/10.1038/138363a0
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