Restoration of valine acceptor activity by combining oligonucleotide fragments derived from a Bacillus subtilis ribonuclease digest of Escherichia coli valine transfer RNA
作者： Kinichiro Oda , Fumiko Kimura , Fumio Harada , Susumu Nishimura
DOI: 10.1016/0005-2787(69)90125-7
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摘要: Abstract Valine tRNA from Escherichia coli , treated with Bacillus subtilis ribonuclease in the presence of Mg 2+ yielded two large fragments. They contained -C-C-A end and pGp end, respectively, could be separated each other by means DEAE-cellulose column chromatography followed rechromatography DEAE-Sephadex A-25 at pH 2.7. When fragments were combined renatured valine acceptor activity was fully restored. It is essential to combine for reactivation activity. No restored either component alone. The restoration temperature time dependent, divalent ion such as also necessary. thermal denaturation ribonuclease-treated occurred quite a lower than that native tRNA. From data profile their reconstituted molecule, possible mechanism renaturation process will discussed.
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