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- W2084107745 abstract "1. Rough endoplasmic reticulum membrane from rat liver was stripped of its ribosomes and was then reacted with liver polyribosomes. Polysomes derived from whole-cell preparations and polysomes free in the cytoplasm were equally effective in providing reconstituted rough endoplasmic reticulum. 2. Reconstituted rough endoplasmic reticulum was tested in vitro for capacity to incorporate amino acids from aminoacyl-tRNA into peptide. The presence of the membrane resulted in a requirement for sulfhydryl compounds not needed by the same polysomes incubated in the absence of membrane. This modification imposed by the presence of the membrane occurred whether the polysomes used for reconstitution were representative of the whole cell population or were polysomes originally free in the cytoplasm. However, polysomes made by adding polyuridylic acid to ribosome subunits did not show this sulfhydryl dependence when used for reconstitution of rough endoplasmic reticulum. This may have been related to the fact that most of these polyuridylic acid complexes were monomers. 3. It is concluded that peptide bond formation by the reconstituted system resembles that of the original rough endoplasmic reticulum freshly prepared from the liver cell in having a sulfhydryl requirement due to the presence of the membrane." @default.
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- W2084107745 date "1972-07-01" @default.
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- W2084107745 title "Role of the endoplasmic reticulum membrane in the sulfhydryl requirement for protein synthesis" @default.
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- W2084107745 doi "https://doi.org/10.1016/0005-2787(72)90399-1" @default.
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