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Role of Steroid Hormones in the Interaction of Polysomes with Endoplasmic Reticulum

Abstract

THE existence of a membrane-bound enzyme which catalyses disulphide interchange has previously been reported1–3. The activity of this enzyme in isolated “rough” fractions of the endoplasmic reticulum is masked when polysomes are attached to the membrane and is observed only when they are removed with, for example, EDTA or aflatoxin B1 (refs. 2 and 3). The same enzyme is also present in fully active form in the “smooth” fractions of the endoplasmic reticulum, but if these are incubated in the presence of polysomes and an appropriate steroid hormone, the enzyme activity decays in time-dependent fashion3.

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References

  1. Goldberg, R. F., Epstein, C. J., and Anfinson, C. B., J. Biol. Chem., 238, 628 (1963).

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  2. Williams, D. J., Gurari, D., and Rabin, B. R., FEBS Lett., 2, 133 (1968).

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  3. Williams, D. J., and Rabin, B. R., FEBS Lett., 4, 103 (1969).

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JAMES, D., RABIN, B. & WILLIAMS, D. Role of Steroid Hormones in the Interaction of Polysomes with Endoplasmic Reticulum. Nature 224, 371–372 (1969). https://doi.org/10.1038/224371a0

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