Abstract
THERE are two opposing conceptions of the native state of proteins in biological fluids. One holds that the native particle is a complex of the various species of proteins present and is altered in the process of isolation. The other supports the independent existence of these species in a state of homogeneous dispersion. Difficulties of separation and inconstancy in amino-acid analyses support the former, and these were encountered1 in efforts to separate and characterize the proteins in hen's egg-white. Block2 has suggested the existence of an ‘orosin’ in egg-white on the basis of the ratio of arginine, histidine and lysine. The evidence from physical methods with blood serum supports the second hypothesis, but these have not been applied to egg-white except for a brief note by Svedberg3 relative to irregularities in the sedimentation constant of native and ‘purified’ ovalbumin.
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References
Young, J. Biol. Chem., 120, 1 (1937).
Block, J. Biol. Chem., 105, 455 (1934).
Svedberg, NATURE, 128, 999 (1931).
Philpot, NATURE, 141, 283 (1938).
Tiselius, Trans. Faraday Soc., 33, 524 (1937).
Hektoen and Cole, J. Infec. Dis., 42, 1 (1928).
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YOUNG, E. Native State of Proteins in Egg-White. Nature 145, 1021 (1940). https://doi.org/10.1038/1451021a0
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DOI: https://doi.org/10.1038/1451021a0
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