Transthyretin mass determination for detection of transthyretin familial amyloid.

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The concentration range of plasma proteins exceeds the dynamic range of any single analytical method. It has been estimated that the concentration range of serum proteins exceeds ten orders of magnitude (1). Because of this, prior immunoselection of even abundant proteins facilitates the relative nonquantitative observations required to show structural abnormality in primary or in posttranslational structure. Determination of atypical proteins by mass measurement has been reported for genetic defects in glycosylation (2, 3) and for monitoring for transthyretin (TTR) defects (4). Here we describe a rapid method of purification and electrospray introduction of TTR into a mass spectrometer to detect mass changes due to amino acid substitutions. The method currently forms the basis for a clinical assay to ascertain TTR mutations resulting in amyloidosis.

Original languageEnglish (US)
Pages (from-to)353-365
Number of pages13
JournalMethods in molecular biology (Clifton, N.J.)
Volume492
DOIs
StatePublished - 2009

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Prealbumin
Amyloid
Blood Proteins
Amyloidosis
Amino Acid Substitution
Glycosylation
Proteins
Mutation

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology

Cite this

Transthyretin mass determination for detection of transthyretin familial amyloid. / O'Brien, John F.; Bergen, Harold Robert (Bob) III.

In: Methods in molecular biology (Clifton, N.J.), Vol. 492, 2009, p. 353-365.

Research output: Contribution to journalArticle

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