Development of quantitative mass spectrometric immunoassay for serum amyloid A

Olgica Trenchevska, Hussein N. Yassine, Chad Borges, Randall W. Nelson, Dobrin Nedelkov

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Objective: Proteins can exist as multiple proteoforms in vivo that can have important roles in physiological and pathological states. Methods: We present the development and characterization of mass spectrometric immunoassay (MSIA) for quantitative determination of serum amyloid A (SAA) proteoforms. Results: Intra- and inter-day precision revealed CVs <10%. Against existing SAA ELISA, the developed MSIA showed good correlation according to the Altman–Bland plot. Individual concentrations of the SAA proteoforms across a cohort of 170 samples revealed 7 diverse SAA polymorphic types and 12 different proteoforms. Conclusion: The new SAA MSIA enables parallel analysis of SAA polymorphisms and quantification of all expressed SAA proteoforms, in a high-throughput and time-efficient manner.

Original languageEnglish (US)
Pages (from-to)743-751
Number of pages9
Issue number8
StatePublished - Nov 16 2016


  • Baseline concentration
  • inflammation biomarker
  • mass spectrometry
  • polymorphism
  • posttranslational modifications
  • proteoforms

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Health, Toxicology and Mutagenesis


Dive into the research topics of 'Development of quantitative mass spectrometric immunoassay for serum amyloid A'. Together they form a unique fingerprint.

Cite this