title: The effect of adjacent residues on the reactivity of tyrosyl with iodine.
abstract: The effect of the adjacent amino acid side chain groups on the iodination rate of the tyrosine was studied. The model peptides used were Gly-Tyr-Gly, Leu-Tyr-Leu, Glu-Tyr-Glu, and Lys-Tyr-Lys, in which the tyrosine is sandwiched between two hydrophobic, two negatively charged, or two positively charged residues. The results show only minor differences in the iodination rate of tyrosine in these four peptides. These differences are very small in comparison with those previously observed between the tyrosines of kappa Bence-Jones proteins.
authors.affiliation: Department of Biochemistry Research, Roswell Park Memorial Institute, New York State Department of Health, Buffalo, N.Y. 14203, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Takeda
authors.forename: B K
authors.initials: BK
authors.lastname: Seon
authors.forename: O A
authors.initials: OA
authors.lastname: Roholt
authors.forename: D
authors.initials: D
authors.lastname: Pressman
mesh_terms: D000595:Amino Acid Sequence; D007455:Iodine / Q000737:chemistry*; D007700:Kinetics; D009842:Oligopeptides / Q000737:chemistry*; D013329:Structure-Activity Relationship; D014443:Tyrosine / Q000737:chemistry*
chemical_list: D009842:Oligopeptides; D014443:Tyrosine; D007455:Iodine