POOLS OF RIBOSOMAL-PROTEINS IN ESCHERICHIA-COLI - STUDIES ON EXCHANGE OF PROTEINS BETWEEN POOLS AND RIBOSOMES
POOLS OF RIBOSOMAL-PROTEINS IN ESCHERICHIA-COLI - STUDIES ON EXCHANGE OF PROTEINS BETWEEN POOLS AND RIBOSOMES
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DOI：
10.1111/j.1432-1033.1975.tb02275.x
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发表时间：
1975-01-01
期刊：
影响因子：
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通讯作者：
NIERHAUS, KH
中科院分区：
文献类型：
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作者：
ULBRICH, B;NIERHAUS, KH
介绍了一种新的标记技术，该技术允许在富培养基中生长时对具有高比活性的细胞成分进行营养。通过该技术，可以在150000 × g离心后的上清液中直接测量每种蛋白质的池大小。发现了S1， S2, S6, S10, L1, L4, L7, L8/9, L10, L12， L21和L25的可测量池。核糖体蛋白从上清液迁移到核糖体（即结合），反之亦然（解离）的实验表明，核糖体的组成具有显著的稳定性。核糖体参与或不参与聚苯醚合成没有显著差异。
A new labelling techniquein vivohas been introduced which allows the tritiation of cell components with high specific activity during growth in rich medium. By this technique the pool size of each protein can be measured directly in the supernatant from centrifugation at 150000 × g. A measurable pool was found for the proteins S1, S2, S6, S10, L1, L4, L7, L8/9, L10, L12, L21, and L25.Experiments on migration of ribosomal proteins from the supernatant to ribosomes (i.e. association) andvice versa(dissociation) demonstrate a remarkable constancy in the composition of the ribosome. There is no significant difference between ribosomes engaged or not engaged in poly‐(Phe) synthesis.