The use of a dipolar ion-exchanger for the fractionation of transfer ribonucleic acid

Transfer ribonucleic acid is well fractionated on columns of arginine-agarose, whose properties appear in general to be similar to those of DEAE-Sephadex. However, the amino acid acceptor species are separated into sharper peaks and in several instances, notably for methionine, glycine, serine, leuc...

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Bibliographic Details
Published in:Nucleic acids research 1976-01, Vol.3 (1), p.177-190
Main Authors: Jay, Francis T., Coultas, Carol, Jones, David S.
Format: Article
Language:English
Subjects:
Escherichia coli
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Summary:Transfer ribonucleic acid is well fractionated on columns of arginine-agarose, whose properties appear in general to be similar to those of DEAE-Sephadex. However, the amino acid acceptor species are separated into sharper peaks and in several instances, notably for methionine, glycine, serine, leucine and aspartate accepting tRNAs from Escherichia coli, isoaccepting species are well resolved. In the case of methionine accepting tRNA from E. coli the tRNAMetm species is eluted before the tRNMetf species and since it is also eluted prior to the bulk of the tRNA it is obtained in a high degree of purity. By comparing the properties of columns of arginineagarose and its methyl ester in which the carboxylate anion is blocked, it is seen that the carboxylate ion plays a role in the fractionation of the tRNAMet species.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/3.1.177