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• W2024798966 abstract "A convenient method to purify each of the non-ribosomal proteins required to translate a native mRNA in vitro is described. In this scheme, the ribosome is used as an 'affinity' matrix to selectively elute the non-ribosomal proteins required for translation that are bound to these particles. Different sets of these proteins can be eluted with solutions of Mg2+ and NH4+ of various concentrations from either 70S, or 30S and 50S particles. A scheme for the purification of each initiation, elongation and release factor and 20 aminoacyl-tRNA synthetases is described. Specific examples of the purification of the initiation (IF-1, IF-2, IF-3) and elongation (EF-Tu and EF-G) factors and for a protein called 'rescue', which affects the association of native ribosomal subunits, are given. A scheme for the purification of EF-P, which stimulates peptide-bond synthesis and one of the W proteins, which permit reconstitution of translation is also described. The procedure markedly simplifies the isolation, in homogeneous form, of all the non-ribosomal proteins required to reconstruct translation." @default.
• W2024798966 created "2016-06-24" @default.
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• W2024798966 date "1996-01-01" @default.
• W2024798966 modified "2023-10-11" @default.
• W2024798966 title "The ribosome as ‘affinity matrix’: Efficient purification scheme for translation factors" @default.
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• W2024798966 doi "https://doi.org/10.1016/0300-9084(96)81329-0" @default.
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