Identification and analysis of kinetically stable proteins in human plasma and red blood cells

Authors
Trasatti, Hannah S.
ORCID
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Other Contributors
Colón, Wilfredo
Cramer, Steven M.
Karande, Pankaj
Makhatadze, George I.
Issue Date
2018-05
Keywords
Chemistry
Degree
PhD
Terms of Use
This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
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Abstract
From a similar analysis of freshly prepared human hemolysate, three non-redundant proteins hemoglobin, catalase, and peroxiredoxin 2 were identified. Hemoglobin is a source of oxidative stress in the red blood cell via its iron ligands, whereas catalase and peroxiredoxin 2 are responsible for the elimination of dangerous reactive oxygen species as part of the antioxidant system. Protein kinetic stability may serve as a protective mechanism in these proteins to preserve their function by preventing misfolding after oxidative damage. Further depletion of human plasma and hemolysate is necessary to get a fuller picture of protein kinetic stability in humans. Due to the large protein abundance disparity in both samples, only a fraction of the proteins was probed for kinetic stability. Development of new methods to specifically deplete non kinetically stable protein out of complex biological samples would address this issue. Alternatively, a technique that is not limited by sample capacity would allow for examination of a broader range of proteins. Overall, the identification of thirteen kinetically stable proteins in human blood suggests that kinetic stability is an important characteristic that has been preserved throughout evolution, even as eukaryotes gained more complex protein function and regulation.
Description
May 2018
School of Science
Department
Dept. of Chemistry and Chemical Biology
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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