A review of quantitative methods for proteomic studies.
An overview is provided of six strategies for relative or absolute quantitation of protein abundances that are widely used in proteomic studies. Strengths and limitations are discussed. Four of these involve stable isotope labeling and isotope ratio measurements by mass spectrometry. In another, mass spectra are used to deconvolute overlapping peptide HPLC peaks to provide relative quantitation based on peak areas. The sixth provides relative abundances of proteins based on 2-D gel arrays. It should be noted that these strategies measure peptide and protein abundances, and cannot directly assess changes in regulation or expression.
Fenselau
Catherine
C
Department of Chemistry & Biochemistry, and Marlene & Stewart Greenebaum Cancer Center, University of Maryland, College Park, MD 20742, USA. fenselau@umd.edu
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D007553:Isotope Labeling; D008954:Models, Biological; D008969:Molecular Sequence Data; D011506:Proteins / Q000032:analysis* / Q000737:chemistry; D040901:Proteomics / Q000379:methods*
D011506:Proteins