Almeida M R, Ferlini A, Forabosco A, Gawinowicz M, Costa P P, Salvi F, Plasmati R, Tassinari C A, Altland K, Saraiva M J
Centro de Estudos de Paramiloidose, Instituto de Ciências Biomédicas, Porto, Portugal.
Hum Mutat. 1992;1(3):211-5. doi: 10.1002/humu.1380010306.
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 DNA 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).
我们报告了两个患有遗传性淀粉样变性的意大利家族中两种新的转甲状腺素蛋白（TTR）变体的生化和分子特征。两个家族均表现出神经病变和心肌病，但在其他临床特征上有所不同。这些TTR变体先前通过等电聚焦（IEF）检测到；一种是中性TTR变体，另一种是碱性变体。通过蛋白质和DNA分析，发现中性变体在多肽链的第49位（TTR Ala-49）有一个苏氨酸残基被丙氨酸取代。碱性变体在第89位（TTR Gln-89）有一个谷氨酰胺残基取代了谷氨酸。
