An inherited non-amyloidogenic transthyretin variant, [Ser6]-TTR, with increased thyroxine-binding affinity, characterized by DNA sequencing.

@article{Fitch1991AnIN,
  title={An inherited non-amyloidogenic transthyretin variant, [Ser6]-TTR, with increased thyroxine-binding affinity, characterized by DNA sequencing.},
  author={Nicholas Samuel Fitch and M. T. Akbari and David Boyer Ramsden},
  journal={The Journal of endocrinology},
  year={1991},
  volume={129 2},
  pages={
          309-13
        }
}
Amplification and sequencing of the four transthyretin (TTR) exons of a subject with a variant TTR with four-fold increased affinity for thyroxine revealed a heterozygous G to A point mutation at base 7 of exon 2. This results in a serine for glycine change at residue 6 of the mature TTR monomer. No other mutations were found in any exon. Amplification and MspI digestion of TTR exon 2 from the leucocyte DNA of eight members of the subject's family revealed that all but one member were also… CONTINUE READING

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The relative amounts of plasma transthyretin forms in familial transthyretin amyloidosis: a quantitative analysis by Fourier transform ion-cyclotron resonance mass spectrometry.

  • Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis
  • 2011
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