Application of semiquantitative proteomics techniques to the maillard reaction.
Proteomic tools-in particular, mass spectrometry (MS)-have advanced significantly in recent years, and the identification of proteins within complex mixtures is now a routine procedure. Quantitative methods of analysis are less well advanced and continue to develop. These include the use of stable isotope ratio approaches, isotopically labeled peptide standards, and nonlabeling methods. This paper summarizes the use of MS as a proteomics tool to identify and semiquantify proteins and their modified forms by using examples of relevance to the Maillard reaction. Finally, some challenges for the future are presented.
Ames
Jennifer M
JM
Hugh Sinclair Unit of Human Nutrition, School of Food Biosciences, The University of Reading, Whiteknights, Reading RG6 6AP, United Kingdom. j.m.ames@reading.ac.uk
D000595:Amino Acid Sequence; D015180:Electrophoresis, Gel, Two-Dimensional; D015416:Maillard Reaction; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010455:Peptides / Q000032:analysis / Q000737:chemistry; D011506:Proteins / Q000032:analysis* / Q000737:chemistry; D020543:Proteome; D011765:Pyruvaldehyde / Q000032:analysis*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D010446:Peptide Fragments; D010455:Peptides; D011506:Proteins; D020543:Proteome; D011765:Pyruvaldehyde