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Radiolytic and enzymatic dimerization of tyrosyl residues in insulin, ribonuclease, papain and collagen

Conference:

Abstract

Insulin ribonuclease, papain and collagen solutions saturated with nitrogen, N/sub 2/O or air were irradiated with doses of 10 to 640 Gy of gamma rays. Protein solutions were also oxidized enzymatically in a system of horse-radish peroxidase: hydrogen peroxide. Column chromatography (Sephadex G-75 or Sephacryl S-200) of treated protein solutions revealed that they contain protein molecular aggregates. Nitrogen saturation of solution before irradiation was most favourable for radiation-induced aggregation of proteins. Fluorescence analysis of protein solutions resulted in detection of dityrosyl structures in irradiated as well as in enzymatically oxidized proteins. Concentration of dityrosine in proteins studied was determined fluorimetrically in their hydrolysates separated on BioGel P-2 column. In irradiated proteins, dityrosine was present almost exclusively in their aggregated forms. In proteins oxidized enzymatically, dityrosine was also present in fractions containing apparently unchanged protein. Mechanisms which could account for differences in the yield of dityrosine formation in radiolysis and in enzymatic oxidation of proteins are suggested.
Authors:
Boguta, G; Dancewicz, A M [1] 
  1. Institute of Nuclear Research, Warsaw (Poland)
Publication Date:
Mar 01, 1983
Product Type:
Conference
Reference Number:
AIX-14-775677; EDB-83-180070
Resource Relation:
Journal Name: Int. J. Radiat. Biol. Relat. Stud. Phys., Chem. Med.; (United Kingdom); Journal Volume: 43:3; Conference: 16. annual meeting of the European Society for Radiation Biology, Krakow (Poland), 8-10 Sep 1981; Other Information: Presented at conference in part only
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; TYROSINE; CHEMICAL RADIATION EFFECTS; DIMERIZATION; AIR; COLLAGEN; DOSE-RESPONSE RELATIONSHIPS; FLUORESCENCE SPECTROSCOPY; GAMMA RADIATION; HYDROGEN PEROXIDE; INSULIN; LIQUID COLUMN CHROMATOGRAPHY; NITROGEN; NITROUS OXIDE; OXIDATION; PAPAIN; RADIOLYSIS; RNA-ASE; AMINO ACIDS; CARBOXYLIC ACIDS; CHALCOGENIDES; CHEMICAL REACTIONS; CHEMISTRY; CHROMATOGRAPHY; DECOMPOSITION; ELECTROMAGNETIC RADIATION; ELEMENTS; EMISSION SPECTROSCOPY; ENZYMES; ESTERASES; FLUIDS; GASES; HORMONES; HYDROGEN COMPOUNDS; HYDROLASES; HYDROXY ACIDS; IONIZING RADIATIONS; NITROGEN COMPOUNDS; NITROGEN OXIDES; NONMETALS; ORGANIC ACIDS; ORGANIC COMPOUNDS; OXIDES; OXYGEN COMPOUNDS; PEPTIDE HORMONES; PEPTIDE HYDROLASES; PEROXIDES; PHOSPHODIESTERASES; POLYMERIZATION; PROTEINS; RADIATION CHEMISTRY; RADIATION EFFECTS; RADIATIONS; SCLEROPROTEINS; SEPARATION PROCESSES; SH-PROTEINASES; SPECTROSCOPY; 560111* - Radiation Effects on Biochemicals- In Vitro- (-1987)
OSTI ID:
5598276
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: IJRBA
Submitting Site:
HEDB
Size:
Pages: 249-265
Announcement Date:
Aug 01, 1983

Conference:

Citation Formats

Boguta, G, and Dancewicz, A M. Radiolytic and enzymatic dimerization of tyrosyl residues in insulin, ribonuclease, papain and collagen. United Kingdom: N. p., 1983. Web.
Boguta, G, & Dancewicz, A M. Radiolytic and enzymatic dimerization of tyrosyl residues in insulin, ribonuclease, papain and collagen. United Kingdom.
Boguta, G, and Dancewicz, A M. 1983. "Radiolytic and enzymatic dimerization of tyrosyl residues in insulin, ribonuclease, papain and collagen." United Kingdom.
@misc{etde_5598276,
title = {Radiolytic and enzymatic dimerization of tyrosyl residues in insulin, ribonuclease, papain and collagen}
author = {Boguta, G, and Dancewicz, A M}
abstractNote = {Insulin ribonuclease, papain and collagen solutions saturated with nitrogen, N/sub 2/O or air were irradiated with doses of 10 to 640 Gy of gamma rays. Protein solutions were also oxidized enzymatically in a system of horse-radish peroxidase: hydrogen peroxide. Column chromatography (Sephadex G-75 or Sephacryl S-200) of treated protein solutions revealed that they contain protein molecular aggregates. Nitrogen saturation of solution before irradiation was most favourable for radiation-induced aggregation of proteins. Fluorescence analysis of protein solutions resulted in detection of dityrosyl structures in irradiated as well as in enzymatically oxidized proteins. Concentration of dityrosine in proteins studied was determined fluorimetrically in their hydrolysates separated on BioGel P-2 column. In irradiated proteins, dityrosine was present almost exclusively in their aggregated forms. In proteins oxidized enzymatically, dityrosine was also present in fractions containing apparently unchanged protein. Mechanisms which could account for differences in the yield of dityrosine formation in radiolysis and in enzymatic oxidation of proteins are suggested.}
journal = {Int. J. Radiat. Biol. Relat. Stud. Phys., Chem. Med.; (United Kingdom)}
volume = {43:3}
place = {United Kingdom}
year = {1983}
month = {Mar}
}