Abstract
ZEIN has been generally considered to be a simple homogeneous protein. By precipitations which followed the addition of successive amounts of pure water to zein solutions, the solvent for which was originally 70 per cent (weight) in ethyl alcohol, it was found that the purified protein could be divided into three distinct and nearly homogeneous fractions, the larger zein molecules having lower solubilities than smaller ones. There has been no evidence of irreversible changes in the state of aggregation of these fractions. The purified whole zein and the fractions have been characterised by their sedimentation constants, diffusion constants, electrophoretic mobilities and dielectric constants.
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References
Wyman, J. Biol. Chem., 90, 443 (1931).
Williams, Trans. Farad. Soc., 30, 723 (1934).
Perrin, J. Phys., VII, 5, 497 (1934).
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WATSON, C., ARRHENIUS, S. & WILLIAMS, J. Physical Chemistry of Zein. Nature 137, 322–323 (1936). https://doi.org/10.1038/137322a0
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DOI: https://doi.org/10.1038/137322a0
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