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

人类生物学氨基酸代谢中的同位素比质谱

• 批准号: 7721443
• 负责人: KEVIN E YARASHESKI
• 金额: $ 0.89万
• 依托单位: WASHINGTON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-02-01 至 2009-01-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721443
• 关键词: Amino Acid Sequence; Amino Acids; Biochemical Process; Chemicals; Computer Retrieval of Information on Scientific Projects Database; Disease; Funding; Gases; Gene Expression; Genome; Genomics; Grant; Human Biology; Institution; Isotopes; Kinetics; Label; Mass Spectrum Analysis; Metabolism; Methodology; Modification; Pathogenesis; Physiological; Protein Biosynthesis; Proteins; Rate; Research; Research Personnel; Resources; Role; Science; Source; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; United States National Institutes of Health; in vivo; novel; protein function; protein structure; synthetic protein

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.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 生物重要蛋白质的全面表征对于生物医学科学的进步至关重要。 MALDI和LC-MS彻底改变了我们表征蛋白质结构、质量、氨基酸序列和化学修饰的方式。 然而，现有的和新的蛋白质的完整表征应包括基因表达，蛋白质合成和降解速率，蛋白质功能的评估。 以这种方式，蛋白质可以在基因组表达、生物化学加工和生理功能的所有水平上表征。 在这一章中，我们讨论了如何稳定标记的氨基酸管理，稀释和掺入方法已与气体同位素比质谱（IRMS）相结合，以定量体内蛋白质的合成和降解率。 这种方法将被应用于许多新的蛋白质，在后基因组时代的识别和表征，使他们的作用，疾病的发病机制可以确定。