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Peptidyl‐tRNA. XIII. The Chromatographic Behavior of Peptidyl‐tRNA val E. Coli on BD‐Cellulose Column
Author(s) -
Ziv E.,
De Groot N.,
Rappoport S.,
Lapidot Y.
Publication year - 1971
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197100036
Subject(s) - transfer rna , chemistry , elution , residue (chemistry) , peptide , chromatography , stereochemistry , biochemistry , rna , gene
The behavior of different peptidyl‐tRNA val 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. Gly n ‐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.