The complexity of protein semiochemistry in mammals. (11th August 2014)

• Record Type: Journal Article
• Authors: Beynon, Robert J.; Armstrong, Stuart D.; Gómez-Baena, Guadalupe; Lee, Victoria; Simpson, Deborah; Unsworth, Jennifer; Hurst, Jane L.
• Is Part Of: Biochemical Society transactions. Volume 42:Number 4(2014)
• Page Start: 837
• Page End: 845
• Publication Date: 2014-08-11
• Subjects: major urinary protein (MUP) -- mass spectrometry -- stable isotope -- QconCAT; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20140133
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : The high degree of protein sequence similarity in the MUPs (major urinary proteins) poses considerable challenges for their individual differentiation, analysis and quantification. In the present review, we discuss MS approaches for MUP quantification, at either the protein or the peptide level. In particular, we describe an approach to multiplexed quantification based on the design and synthesis of novel proteins (QconCATs) that are concatamers of quantification standards, providing a simple route to the generation of a set of stable-isotope-labelled peptide standards. The MUPs pose a particular challenge to QconCAT design, because of their sequence similarity and the limited number of peptides that can be used to construct the standards. Such difficulties can be overcome by careful attention to the analytical workflow.