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.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 生物学上重要的蛋白质的全面表征对于生物医学科学的发展至关重要。 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。 但是，现有蛋白质和新型蛋白质的完全表征应包括评估基因表达，蛋白质合成和降解速率以及蛋白质功能。 以这种方式，蛋白质可以在所有级别的基因组表达，生化加工和生理功能上进行表征。 在本章中，我们将讨论稳定标记的氨基酸给药，稀释和掺入方法与气体同位素比质谱（IRMS）结合使用，以定量体内蛋白质合成和降解速率。 这种方法将应用于在基因组后时代鉴定和表征的许多新型蛋白质，以便可以鉴定出它们在疾病发病机理中的作用。