Proteome turnover in the bloodstream and procyclic forms of Trypanosoma brucei measured by quantitative proteomics.
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ABSTRACT: Background: Cellular proteins vary significantly in both abundance and turnover rates. These parameters depend upon their rates of synthesis and degradation and it is useful to have access to data on protein turnover rates when, for example, designing genetic knock-down experiments or assessing the potential usefulness of covalent enzyme inhibitors. Little is known about the nature and regulation of protein turnover in Trypanosoma brucei, the etiological agent of human and animal African trypanosomiasis. Methods: To establish baseline data on T. brucei proteome turnover, a Stable Isotope Labelling with Amino acids in Cell culture (SILAC)-based mass spectrometry analysis was performed to reveal the synthesis and degradation profiles for thousands of protei
SUBMITTER: Tinti M
PROVIDER: S-EPMC6816455 | biostudies-literature | 2019
REPOSITORIES: biostudies-literature
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