Two transthyretin variants (TTR Ala-49 and TTR Gln-89) in two sicilian kindreds with hereditary amyloidosis
✍ Scribed by Maria do Rosário Almeida; Alessandra Ferlini; Antonino Forabosco; Maryann Gawinowicz; Pedro P. Costa; Fabrizio Salvi; Rosaria Plasmati; Carlo A. Tassinari; Klaus Altland; Maria Joã Saraiva
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 428 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1059-7794
No coin nor oath required. For personal study only.
✦ Synopsis
G e m n y (K. A. 1 Communicated by Steve S. Sommer We report the biochemical and molecular characterization of two new transthyretin (TTR) variants in two Italian families with hereditary amyloidosis. Both families presented neuropathy and cardiomyopathy but they differ in other clinical features. These TTR variants were previously detected by isoelectric focusing (IEF); one is a neutral TTR variant and the other one is basic. By protein and D N A analysis the neutral variant was found to have a substitution of an alanine for a threonine residue at position 49 (TTR Ala-49) of the polypeptide chain. The basic variant has a glutamine residue replacing glutamate at position 89 (TTR Gln-89). o 1992 WiIey-Liss, Inc.