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The complexity of protein semiochemistry in mammals.
Beynon, Robert J; Armstrong, Stuart D; Gómez-Baena, Guadalupe; Lee, Victoria; Simpson, Deborah; Unsworth, Jennifer; Hurst, Jane L.
Afiliação
  • Beynon RJ; *Protein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, U.K.
  • Armstrong SD; *Protein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, U.K.
  • Gómez-Baena G; *Protein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, U.K.
  • Lee V; *Protein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, U.K.
  • Simpson D; *Protein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, U.K.
  • Unsworth J; *Protein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, U.K.
  • Hurst JL; †Mammalian Behaviour and Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, Cheshire CH64 7TE, U.K.
Biochem Soc Trans ; 42(4): 837-45, 2014 Aug.
Article em En | MEDLINE | ID: mdl-25109966
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.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Espectrometria de Massas / Proteínas Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Espectrometria de Massas / Proteínas Idioma: En Ano de publicação: 2014 Tipo de documento: Article