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Über die Ribosomen aus Blättern von Allium porrum

Ehring, Ruth
Zeitschrift für Naturforschung B 2014 v.17 no.12 pp. 837-847
Allium porrum, RNA, animal tissues, arginine, centrifugation, chloroplasts, detergents, leaves, lysine, moieties, phenol, ribosomal proteins, ribosomes, sediments, serine, structural proteins
Plant ribosomes prepared from growing leaves of Allium porrum were purified by differential centrifugation. Isolated ribosomes had a sedimentation constant of 79 —80 S and a ribonucleic acid content of at least 34% dry weight. The ribonucleic acid could be separated from the protein moiety by detergent treatment and was found to sediment as three fractions with sedimentation constants of 27 S, 9-10 S and 5 —6 S respectively. Similar ribonucleic acid components were obtained by phenol treatment of unfractionated leaf homogenates.A comparison of the nucleotide and amino acid composition of Allium porrum ribosomes with data reported for ribosomes from other plant and animal tissues revealed no significant differences. However, the lysine and arginine content of Allium porrum ribosomal protein was found to be significantly greater than that reported for the structural protein of the chloroplasts of the same species.Analysis of the amino terminal end groups of the Allium porrum ribosomal protein yielded predominantly serine.