R
Rodney L. Levine
Researcher at National Institutes of Health
Publications - 200
Citations - 27323
Rodney L. Levine is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Methionine & Methionine sulfoxide reductase. The author has an hindex of 69, co-authored 194 publications receiving 25768 citations. Previous affiliations of Rodney L. Levine include University of California, San Francisco.
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Book ChapterDOI
Determination of carbonyl content in oxidatively modified proteins.
Rodney L. Levine,Donita Garland,Cynthia N. Oliver,Adolfo Amici,Isabel Climent,Anke-G. Lenz,Bong-Whan Ahn,Shmuel Shaltiel,Earl R. Stadtman +8 more
TL;DR: This chapter discusses methods to determine carbonyl content in oxidatively modified proteins and quantitated protein-bound pyruvoyl groups through formation of a Schiff base with p-aminobenzoic acid followed by reduction with cyanoborohydride.
Book ChapterDOI
Carbonyl assays for determination of oxidatively modified proteins
TL;DR: New methods for determination ofcarbonyl content are presented, which are based on the reaction of carbonyl groups with 2,4-dinitrophenylhydrazine to form a 2, 4-d Initrophenolhydrazone, which provide substantial improvements in both sensitivity and specificity.
Journal ArticleDOI
Free radical-mediated oxidation of free amino acids and amino acid residues in proteins.
TL;DR: It is evident that the cyclic oxidation and reduction of the sulfur-containing amino acids may serve as an important antioxidant mechanism, and also that these reversible oxidations may provide an important mechanism for the regulation of some enzyme functions.
Journal ArticleDOI
Methionine residues as endogenous antioxidants in proteins
TL;DR: This work proposes that methionine residues constitute an important antioxidant defense mechanism, and investigates the effect of hydrogen peroxide exposure upon glutamine synthetase from Escherichia coli as an in vitro model system.
Journal ArticleDOI
Carbonyl modified proteins in cellular regulation, aging, and disease,
TL;DR: In eukaryotes, removal is usually carried out by the proteosome, which selectively degrades oxidatively modified proteins, whether they be damaged by reactive oxygen species or specifically oxidized by cellular regulatory processes as mentioned in this paper.