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N ‐tosyl‐L‐phenylalanylchloromethane reacts with cysteine 81 in the molecule of elongation factor Tu from Escherichia coli
Author(s) -
Jonák Jiří,
Petersen Torben E.,
Clark Brian F.C.,
Rychlík Ivan
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80795-3
Subject(s) - tosyl , edman degradation , chemistry , escherichia coli , cysteine , trypsin , residue (chemistry) , peptide , elongation factor , biochemistry , cyclic peptide , chromatography , peptide sequence , stereochemistry , enzyme , ribosome , rna , gene
Elongation factor EF‐Tu from Escherichia coli was labelled with N ‐[ 14 C]tosyl‐L‐phenylalanylchloromethane, digested with trypsin and the peptides obtained separated by HPLC. The only radioactive peak recovered corresponded to tryptic peptide containing residues 75–98. Sequencing of the peptide by automated Edman degradation identified cysteine 81 as the site of N ‐tosyl‐L‐phenylalanylchloromethane modification. These results confirm the importance of this residue for the interaction with aminoacyl‐tRNAs.