Peptidyl‐tRNA. XIII. The Chromatographic Behavior of Peptidyl‐tRNAvalE. Coli on BD‐Cellulose Column

E. Ziv*, N. De Groot, S. Rappoport, Y. Lapidot

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The behavior of different peptidyl‐tRNAval from E. coli on benzoylated DEAE cellulose column is described. It was found that the elution pattern of N‐acetyl‐val‐tRNA differs from that of val‐tRNA. Glyn‐val‐tRNA (n = 2,3) and lys‐gly‐val‐tRNA are eluted from the column differently from val‐tRNA. Blocking of the free amino group of the peptide attached to the tRNA causes a further shift of the elution pattern. Val‐gly‐val‐tRNA and phe‐gly‐val‐tRNA are strongly retarded on the column as compared with val‐tRNA, probably because of the hydrophobic interaction between the peptidyl residue and the BD‐cellulose. It is suggested that the differences in the chromatographic behavior of the different tRNA derivatives are due at least partially to differences in conformation.

Original languageEnglish
Pages (from-to)243-249
Number of pages7
JournalIsrael Journal of Chemistry
Volume9
Issue number2
DOIs
StatePublished - 1971

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