Identification of a new transthyretin variant (Ile49) in familial amyloidotic polyneuropathy using electrospray ionization mass spectrometry and nonisotopic RNase cleavage assay

Masaaki Nakamura, Taro Yamashita, Yukio Ando, Kamran Hamidi Asl, Kazuhiro Tashima, Per Ingvar Ohlsson, Yukio Kususe, Merrill D. Benson

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Mutation of the transthyretin (TTR) plasma protein and gene in a Japanese patient with amyloid polyneuropathy was investigated by electrospray ionization mass spectrometry (ESI-MS) and nonisotopic RNase cleavage assay (NIRCA), respectively. ESI-MS analysis showed normal TTR peaks and additionally a variant TTR with 12-dalton-higher molecular weight than normal TTR. NIRCA suggested that the mutation existed near either the 5' or 3' end of exon 3. Direct DNA sequencing revealed both a normal ACC (threonine) and a variant ATC (isoleucine) at codon 49, which was located near the 5' end of exon 3. The molecular weight shift of this mutation was 12 D, consistent with the result of ESI-MS.

Original languageEnglish (US)
Pages (from-to)186-189
Number of pages4
JournalHuman Heredity
Volume49
Issue number4
DOIs
StatePublished - Jul 1999

Keywords

  • Electrospray ionization mass spectrometry
  • Familiar amyloidotic polyneuropathy
  • Ile49
  • Nonisotopic RNase cleavage assay
  • Transthyretin

ASJC Scopus subject areas

  • Genetics(clinical)

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