Linked Life Data

8405458

Source:http://linkedlifedata.com/resource/pubmed/id/8405458

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-11-19
pubmed:abstractText
We report a promising finding that oxidative modification of proteins by free radicals could be monitored by the formation of oxidized histidine that is detectable by reverse-phase HPLC with electrochemical detection (HPLC-ECD). When the N-protected histidine derivative (N-benzoylhistidine) was exposed to a free radical-generating system (copper/ascorbate), a number of products were detected by HPLC-ECD and the main product among them was found to be identical to N-benzoyl-2-oxo-histidine. The acid hydrolysis of N-benzoyl-2-oxo-histidine provided a single product (2-oxo-histidine) that was detected sensitively by HPLC-ECD. Thus 2-oxo-histidine was indeed generated as the main product in the oxidatively modified proteins by free radicals. Taken together, 2-oxo-histidine may be a useful biological marker for assessing protein modifications under oxidative stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
332
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
208-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
2-Oxo-histidine as a novel biological marker for oxidatively modified proteins.
pubmed:affiliation
Laboratory of Food and Biodynamics, Nagoya University School of Agriculture, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't