Abstract
WHEN lenses of young rats are cooled below 10° C they become reversibly opaque due to the precipitation of a cold-precipitable protein. This fraction is prepared by homogenizing rat lenses in several volumes of water and cooling the 105,000g supernatant to 0° C. Repeated solubilization at 20° C and precipitation at 0° C serves as a means of purification1. The cold-precipitation phenomenon is thought to be caused by changes in protein conformation due to a disturbance of the balance between hydrogen and hydrophobic bonding of protein chains at lower temperatures.
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References
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Zigman, S., and Lerman, S., Exp. Eye Res., 4 (1964).
Zigman, S., Munro, J., and Lerman, S., Biol. Bull., 127 (1964).
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ZIGMAN, S., MUNRO, J. & LERMAN, S. Effect of Urea on the Cold Precipitation of Protein in the Lens of the Dogfish. Nature 207, 414–415 (1965). https://doi.org/10.1038/207414b0
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DOI: https://doi.org/10.1038/207414b0
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