ISOTOPE RATIO MASS SPECT IN HUMAN BIOLOGY AMINO ACID METABOLISM & KINETICS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. A comprehensive characterization of biologically important proteins is critical to the advancement of biomedical science. MALDI- and LC-MS have revolutionized the manner in which we characterize protein structure, mass, amino acid sequence, and chemical modifications. However, complete characterization of existing and novel proteins should include assessments of gene expression, protein synthetic and degradation rates, and protein function. In this manner, proteins can be characterized on all levels of genomic expression, biochemical processing and physiologic function. In this chapter, we discuss how stable-labeled amino acid administration, dilution, and incorporation methodologies have been combined with gas isotope ratio mass spectrometry (IRMS) to quantitate in vivo protein synthesis and degradation rates. This approach will be applied to many of the novel proteins that are identified and characterized in the post-genome era, so that their role in the pathogenesis of disease can be identified.