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Quantitative analysis of the yeast proteome by incorporation of isotopically labeled leucine.

Author(s): Jiang H, English AM

J Proteome Res. 2002 Jul-Aug;1(4):345-50 Authors: Jiang H, English AM

Article GUID: 12645890
Evaluation of D10-Leu metabolic labeling coupled with MALDI-MS analysis in studying the response of the yeast proteome to H2O2 challenge

Author(s): Jiang H; English AM;

An efficient D10-Leu metabolic-labeling method combined with isotope-ratio quantitation by MALDI-TOF MS was used to probe the response of the yeast proteome to H2O2. Control cultures correct for effects not associated with H2O2 challenge. A stress-response ...

Article GUID: 17022625
Progress and Challenges in Ocean Metaproteomics and Proposed Best Practices for Data Sharing.

Author(s): Saito MA, Bertrand EM, Duffy ME, Gaylord DA, Held NA, Hervey WJ, Hettich RL, Jagtap PD, Janech MG, Kinkade DB, Leary DH, McIlvin MR, Moore E...

J Proteome Res. 2019 Apr 05;18(4):1461-1476 Authors: Saito MA, Bertrand EM, Duffy ME, Gaylord DA, Held NA, Hervey WJ, Hettich RL, Jagtap PD, Janech MG, Kinkade DB, Leary DH, McIlvin MR, Moore EK, ...

Article GUID: 30702898
Title:Evaluation of D10-Leu metabolic labeling coupled with MALDI-MS analysis in studying the response of the yeast proteome to H2O2 challenge
Authors:Jiang H,  English AM, 
Link:https://pubmed.ncbi.nlm.nih.gov/17022625/
DOI:10.1021/pr060019m
Category:J Proteome Res
PMID:17022625
Dept Affiliation: CBAMS
1 Centre for Biological Applications of Mass Spectrometry, Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, Canada H4B 1R6.

Description:

An efficient D10-Leu metabolic-labeling method combined with isotope-ratio quantitation by MALDI-TOF MS was used to probe the response of the yeast proteome to H2O2. Control cultures correct for effects not associated with H2O2 challenge. A stress-response index to H2O2 (SRIH2O2) is defined, and values are reported for seven proteins at 45-225 min following exposure to 0.4 mM H2O2. The time course of protein accumulation in unstressed cells following the H10- to D10-SCD switch suggests that proteome responses at <45 min could be monitored by addition of excess D10-Leu to H10-cultures.