The complexity of protein semiochemistry in mammals

Author:

Beynon Robert J.1,Armstrong Stuart D.1,Gómez-Baena Guadalupe1,Lee Victoria1,Simpson Deborah1,Unsworth Jennifer1,Hurst Jane L.2

Affiliation:

1. Protein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, U.K.

2. Mammalian Behaviour and Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, Cheshire CH64 7TE, U.K.

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.

Publisher

Portland Press Ltd.

Subject

Biochemistry

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