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Open Access Green as soon as Postprint is submitted to ZB.
Determination of Carbonyl Groups in Oxidatively Modified Proteins by Reduction with Tritiated Sodium Borohydride.
Anal. Biochem. 177, 419-425 (1989)
Oxidatively modified proteins have been implicated in a variety of physiologic and pathologic processes. Oxidative modification typically causes inactivation of enzymes and also the introduction of carbonyl groups into amino acid side chains of the protein. We describe a method to quantify oxidatively modified proteins through reduction of these carbonyl groups with tritiated borohydride. The technique was applied to purified, oxidatively modified glutamine synthetase and to bronchoalveolar lavage fluid from dogs and from humans. Since the protein content of lung lavage fluid is low, a very sensitive method was required to measure the oxidized residues. Reduction of the carbonyl group generated during oxidation of proteins with tritiated borohydride provided excellent sensitivity. Incorporation of tritium was directly proportional to the amount of protein with a range from 10 to 1000 micrograms. Should moieties other than amino acids be labeled, they are easily removed by rapid benchtop hydrolysis of the protein followed by chromatography on Dowex 50.
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Publication type
Article: Journal article
Document type
Scientific Article
ISSN (print) / ISBN
0003-2697
e-ISSN
1096-0309
Journal
Analytical Biochemistry
Quellenangaben
Volume: 177,
Issue: 2,
Pages: 419-425
Publisher
Elsevier
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Radiation Protection (ISS)