Tryptophan.yl Transfer Ribonucleic Acid Synthetase of Eschwichicz: ‘coli CHARACTER OE; REQUIRED THIOL GROUP AND STRUCTURE OF THIOL PEPTIDES*

@inproceedings{KCJEHL2002TryptophanylTR,
  title={Tryptophan.yl Transfer Ribonucleic Acid Synthetase of Eschwichicz: ‘coli CHARACTER OE; REQUIRED THIOL GROUP AND STRUCTURE OF THIOL PEPTIDES*},
  author={GARY V. KCJEHL and M Lee and KARL H. MIJENCH},
  year={2002}
}
  • GARY V. KCJEHL, M Lee, KARL H. MIJENCH
  • Published 2002
by reductive removal of the thionitrobenzoate with dithiothreitol. Iodoacetamide and N-ethylmaleimide also react with the thiol group required for enzyme activity, but iodoacetic acid inactivates the enzyme through another mechanism. Three or 4 half-cystine residues/subunit were detected by amino acid analysis and by titration of the denatured enzyme with 5,5’-dithiobis(2-nitrobenzoic acid); no disulfide bonds were detected by borohydride reduction. Cleavage of the subunit (molecular weight 37… CONTINUE READING