You need JavaScript to view this

Spin-trapping and ESR studies of the direct photolysis of aromatic amino acids, dipeptides, tripeptides and polypeptides in aqueous solutions-II. Tyrosine and related compounds

Abstract

The UV-photolysis of peptides containing tyrosine (Tyr) was investigated in aqueous solutions at room temperature at 220 and 265 nm. The short-lived free radicals formed during photolysis were spin-trapped by t-nitrosobutane and identified by electron spin resonance. For N-acetyl-and N-formyl-L-Tyr and for peptides containing L-Tyr as the middle residue, photolysis at 265 nm under neutral conditions produced mainly spin-adducts due to the scission between the alpha carbon and the methylene group attached to the aromatic ring, while at 220 nm decarboxylation radicals were spin-trapped. Photolysis of di- and tripeptides at 275 nm in alkaline solutions predominantly generated deamination radicals. The radicals produced in the photolysis of the oxidized A chain of insulin were tentatively characterized by comparison with the results for di- and tripeptides.
Authors:
Lion, Y; Kuwabara, M; Riesz, P [1] 
  1. National Cancer Inst., Bethesda, MD (USA)
Publication Date:
Jan 01, 1982
Product Type:
Journal Article
Reference Number:
AIX-13-674727; EDB-82-116104
Resource Relation:
Journal Name: Photochem. Photobiol.; (United Kingdom); Journal Volume: 35:1
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; PEPTIDES; PHOTOLYSIS; TYROSINE; AQUEOUS SOLUTIONS; ELECTRON SPIN RESONANCE; PHOTOCHEMISTRY; RADICALS; ULTRAVIOLET RADIATION; AMINO ACIDS; CARBOXYLIC ACIDS; CHEMICAL REACTIONS; CHEMISTRY; DECOMPOSITION; DISPERSIONS; ELECTROMAGNETIC RADIATION; HYDROXY ACIDS; MAGNETIC RESONANCE; MIXTURES; ORGANIC ACIDS; ORGANIC COMPOUNDS; PHOTOCHEMICAL REACTIONS; PROTEINS; RADIATIONS; RESONANCE; SOLUTIONS; 560111* - Radiation Effects on Biochemicals- In Vitro- (-1987)
OSTI ID:
5283085
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: PHCBA
Submitting Site:
HEDB
Size:
Pages: 43-52
Announcement Date:

Citation Formats

Lion, Y, Kuwabara, M, and Riesz, P. Spin-trapping and ESR studies of the direct photolysis of aromatic amino acids, dipeptides, tripeptides and polypeptides in aqueous solutions-II. Tyrosine and related compounds. United Kingdom: N. p., 1982. Web. doi:10.1111/j.1751-1097.1982.tb03809.x.
Lion, Y, Kuwabara, M, & Riesz, P. Spin-trapping and ESR studies of the direct photolysis of aromatic amino acids, dipeptides, tripeptides and polypeptides in aqueous solutions-II. Tyrosine and related compounds. United Kingdom. doi:10.1111/j.1751-1097.1982.tb03809.x.
Lion, Y, Kuwabara, M, and Riesz, P. 1982. "Spin-trapping and ESR studies of the direct photolysis of aromatic amino acids, dipeptides, tripeptides and polypeptides in aqueous solutions-II. Tyrosine and related compounds." United Kingdom. doi:10.1111/j.1751-1097.1982.tb03809.x. https://www.osti.gov/servlets/purl/10.1111/j.1751-1097.1982.tb03809.x.
@misc{etde_5283085,
title = {Spin-trapping and ESR studies of the direct photolysis of aromatic amino acids, dipeptides, tripeptides and polypeptides in aqueous solutions-II. Tyrosine and related compounds}
author = {Lion, Y, Kuwabara, M, and Riesz, P}
abstractNote = {The UV-photolysis of peptides containing tyrosine (Tyr) was investigated in aqueous solutions at room temperature at 220 and 265 nm. The short-lived free radicals formed during photolysis were spin-trapped by t-nitrosobutane and identified by electron spin resonance. For N-acetyl-and N-formyl-L-Tyr and for peptides containing L-Tyr as the middle residue, photolysis at 265 nm under neutral conditions produced mainly spin-adducts due to the scission between the alpha carbon and the methylene group attached to the aromatic ring, while at 220 nm decarboxylation radicals were spin-trapped. Photolysis of di- and tripeptides at 275 nm in alkaline solutions predominantly generated deamination radicals. The radicals produced in the photolysis of the oxidized A chain of insulin were tentatively characterized by comparison with the results for di- and tripeptides.}
doi = {10.1111/j.1751-1097.1982.tb03809.x}
journal = {Photochem. Photobiol.; (United Kingdom)}
volume = {35:1}
journal type = {AC}
place = {United Kingdom}
year = {1982}
month = {Jan}
}