Comparison of proteins bound to the different functional classes of messenger RNA

Proteins from nuclear ribonucleoproteins, informosomes, polysomal messenger ribonucleoproteins and cytoplasmic "binding factor" are characterized. 1. Nuclear ribonucleoproteins are purified from nuclei disrupted by ultrasonication. Possible contamination by nucleoplasm, histones or remaining cytoplasmic structures is controlled. 2. Informosomal proteins are obtained by mild RNAase degradation. This method gives informosomal proteins without appreciable contamination. 3. Polysomal messenger ribonucleoproteins are obtained from cells where the initiation of protein synthesis is arrested in order to release the messenger ribonucleoproteins from the polysomes. Their proteins are obtained like the informosomal proteins by mild RNAase digestion. No contamination by informosomes could be detected by sodium dodecyl sulfate gel electrophoresis. 4. Cytoplasmic "binding factor" proteins are purified by affinity chromatography. 5. The four sets of proteins are analysed by sodium dodecylsulfate acrylamide gel electrophoresis. In spite of the fact that some proteins from one or another kind of messenger ribonucleoprotein, have apparently the same molecular weight, the majority of proteins differ.