Abstract
FROM their ultracentrifugal studies on thyroglobulin, Heidelberger and Pedersen1 found that solutions of this protein within its pH stability region2 are fairly homogeneous (Fig. 1). The sedimentation picture shows, in addition to a predominating component consisting of molecules having a molecular weight of about 700,000, a small amount of heavier and lighter molecules with poorly defined sedimentation boundaries. These molecules were assumed to have been formed respectively by the dissociation and association of the molecules comprising the predominating component. It was noticed that on dilution the number of lower molecular weight molecules increased.
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References
M. Heidelberger and K. O. Pedersen, J. Gen. Physiol., 19, 95 (1935).
M. Heidelberger and T. Svedberg, Science, 80, 414 (1934).
M. Heidelberger and W. Palmer, J. Biol. Chem., 101, 433 (1933).
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LUNDGREN, H. Association and Dissociation Reactions of Thyroglobulin. Nature 138, 122 (1936). https://doi.org/10.1038/138122a0
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DOI: https://doi.org/10.1038/138122a0
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