Analysis of intact protein isoforms by mass spectrometry

Jeremiah D. Tipton, John C. Tran, Adam D. Catherman, Dorothy R. Ahlf, Kenneth R. Durbin, Neil L. Kelleher*

*Corresponding author for this work

Research output: Contribution to journalShort surveypeer-review

79 Scopus citations

Abstract

The diverse proteome of an organism arises from such events as single nucleotide substitutions at the DNA level, different RNA processing, and dynamic enzymatic post-translational modifications. This minireview focuses on the measurement of intact proteins to describe the diversity found in proteomes. The field of biological mass spectrometry has steadily advanced, enabling improvements in the characterization of single proteins to proteins derived from cells or tissues. In this minireview, we discuss the basic technology for "top-down" intact protein analysis. Furthermore, examples of studies involved with the qualitative and quantitative analysis of full-length polypeptides are provided.

Original languageEnglish (US)
Pages (from-to)25451-25458
Number of pages8
JournalJournal of Biological Chemistry
Volume286
Issue number29
DOIs
StatePublished - Jul 22 2011

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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