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- W1966069400 abstract "1. Ribosomal proteins extracted with LiCl-urea from different tissues of the same animal appear similar upon acrylamide-gel electrophoresis. Within a given tissue, ribosomal proteins isolated from monosomes and from polysomes of different aggregate size are electrophoretically similar. 2. Ribosomal proteins isolated from the same tissue of animals of various orders and genera yield different electrophoretic patterns. 3. All the protein components present in the electrophoretic patterns of intact (80 S) ribosomes are individually represented in both the ‘derived’ (47 S) and the ‘native’ (60 S) large ribosomal subunits. 4. The electrophoretic patterns of proteins isolated from the small (32 S) ribosomal subunits are generally less complex than those isolated from their complementary large (47 S) subunits. However, it has been found that the ‘32-S patterns’ obtained from different tissues of the same animal appear dissimilar both from one another and from the patterns of the corresponding ‘native’ small ribosomal subunits. This dissimilarity could be due to some phenomenon, as yet unknown, during dissociation of ribosomes with EDTA." @default.
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- W1966069400 date "1968-10-01" @default.
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- W1966069400 title "The protein composition of ribosomes and ribosomal subunits from animal tissues. Electrophoretic studies" @default.
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- W1966069400 doi "https://doi.org/10.1016/0005-2795(68)90142-6" @default.
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