Gary N. Wells

Leonard Beevers

1. Proteinaceous factors contained in a 0.5m-KCl extract of ribosomes from pea cotyledons form a ternary complex at 0°C with [14C]phenylalanyl-tRNA and poly(U). The complex is measured by its quantitative retention on Millipore filters. 2. Complex-assembly is optimal at 5mm-Mg2+ and is independent of GTP and ribosomes. 3. The addition of ribosomes is required to stabilize the complex at 34°C. The complex binds to a puromycin-sensitive site on the ribosome. 4. Soluble factors from the 250000g supernatant of pea cotyledon form a Millipore-retainable complex dependent on GTP and ribosomes. 5. Complex-formation by soluble factors has a Mg2+ optimum of 10–12mm and forms a puromycin-insensitive complex with ribosomes. 6. The function of the ribosomal protein factors and the supernatant fraction in initiation of protein synthesis is discussed.</jats:p

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Biochemical Journal

Protein synthesis in the cotyledons of <i>Pisum sativum</i> L. Protein factors involved in the binding of phenylalanyl-transfer ribonucleic acid to ribosomes

http://www.biochemj.org/content/ppbiochemj/139/1/61.full.pdf

Protein synthesis in the cotyledons of Pisum sativum L. Protein factors involved in the binding of phenylalanyl-transfer ribonucleic acid to ribosomes*

Protein synthesis in the cotyledons of Pisum sativum L. Protein factors involved in the binding of phenylalanyl-transfer ribonucleic acid to ribosomes*

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