High-throughput affinity mass spectrometry.

Urban A. Kiernan, Dobrin Nedelkov, Eric E. Niederkofler, Kemmons A. Tubbs, Randall W. Nelson

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Affinity mass spectrometry (AMS) is a proteomics approach for selectively isolating target protein(s) from complex biological fluids for mass spectrometric analysis. The resulting high-content mass spectrometry (MS) data show the unique MS protein signatures (wild-type, posttranslationally modified, as well as genetically modified forms of the protein target) that are present within a biological sample. Information regarding such protein diversity is normally lost in classical proteomic or immunoassay analyses. This chapter presents a step-by-step description of high-throughput AMS in the population proteomic screening of the human plasma protein cystatin C.

Original languageEnglish (US)
Pages (from-to)141-150
Number of pages10
JournalMethods in molecular biology (Clifton, N.J.)
Volume328
StatePublished - 2006

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ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Kiernan, U. A., Nedelkov, D., Niederkofler, E. E., Tubbs, K. A., & Nelson, R. W. (2006). High-throughput affinity mass spectrometry. Methods in molecular biology (Clifton, N.J.), 328, 141-150.