Linked Life Data

9396084

Source:http://linkedlifedata.com/resource/pubmed/id/9396084

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-1-21
pubmed:abstractText
Generation of reactive oxygen species in vivo results in oxidative-damage to cellular components, including proteins. Due to the relatively long half-lives of several blood proteins the cumulative formation of oxidatively damaged proteins might serve as a biomarker for reactive oxygen species formation. The most prominent sources of reactive oxygen species in vivo are site-specific metal ion-catalyzed reactions of the Fenton and Haber-Weiss types and the H2O2/peroxidase system. In vitro oxidation of L-tyrosine using a peroxidase or Cu++/H2O2 system gives rise to the formation of a highly fluorescent substance, bityrosine. High-performance liquid chromatography (HPLC) analysis of acid hydrolyzed serum albumin after oxidation with peroxidase/H2O2 or with Cu++/H2O2 showed that bityrosine had been formed whereas oxidation of this protein with Fe(III)/ascorbate did not result in the formation of bityrosine. Bityrosine could not be detected in human plasma proteins or haemoglobin with the detection limit of one pmol per mg protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0901-9928
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
205-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Analysis of native human plasma proteins and haemoglobin for the presence of bityrosine by high-performance liquid chromatography.
pubmed:affiliation
Institute of Toxicology, National Food Agency of Denmark, Søborg, Denmark.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't