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Development of the Proteolytic 18O Labeling Method for Comparative Proteomics

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Air date: Tuesday, March 11, 2003, 2:00:00 PM
Time displayed is Eastern Time, Washington DC Local
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Category: Mass Spectrometry
Runtime: 00:55:09
Description: As the sequencing is completed of many species' genomes, the study of the protein compliment to the genome, or the proteome, has emerged as a dynamic field of research. A common approach to characterizing changed states is comparative proteomics, in which the relative amounts of proteins present in two or more samples are compared. In order to determine the relative amount of the proteins present, a proteolytic method for 18O labeling can be used. Briefly, pools of proteins are enzymatically digested in parallel in H216O and H218O. In the latter pool two atoms of 18O are incorporated into the carboxyl-terminus of each new peptide. Comparative proteomic studies can be performed by mixing the unlabeled peptide pool (generated in H216O) and the isotope labeled peptide pool (from H218O) and analyzing the peptide pairs by mass spectrometry.

Mass Spectrometry Interest Group of the NCI at Frederick
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NLM Title: Development of the proteolytic 18O labeling method for comparative proteomics [electronic resource] / Kristy J. Reynolds.
Author: Reynolds, Kristy J.
National Institutes of Health (U.S.)
Publisher:
Abstract: (CIT): As the sequencing is completed of many species' genomes, the study of the protein compliment to the genome, or the proteome, has emerged as a dynamic field of research. A common approach to characterizing changed states is comparative proteomics, in which the relative amounts of proteins present in two or more samples are compared. In order to determine the relative amount of the proteins present, a proteolytic method for 18O labeling can be used. Briefly, pools of proteins are enzymatically digested in parallel in H216O and H218O. In the latter pool two atoms of 18O are incorporated into the carboxyl-terminus of each new peptide. Comparative proteomic studies can be performed by mixing the unlabeled peptide pool (generated in H216O) and the isotope labeled peptide pool (from H218O) and analyzing the peptide pairs by mass spectrometry. Mass Spectrometry Interest Group of the NCI at Frederick.
Subjects: Drug Resistance
Mass Spectrometry
Proteomics
Publication Types: Webcasts
Rights: This is a work of the United States Government. No copyright exists on this material. It may be disseminated freely.
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NLM Classification: QU 58.5
NLM ID: 101267827
CIT Live ID: 2322
Permanent link: http://videocast.nih.gov/launch.asp?10740