期刊
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
卷 10, 期 3, 页码 190-197出版社
PARTHENON PUBLISHING GROUP
DOI: 10.3109/13506120308999000
关键词
transthyretin variants; on-line analysis; immunoaffinity; mass spectrometry
We report here for the first time the on-line analysis of transthyretin genetic variants by mass spectral analysis. The use of mass spectrometry to analyze immunoprecipitated transthyretin has been previously described. However, the on-line analysis of TTR directly from serum reported here will allow for a fully automated high throughput analysis. Mutations in the plasma tranport protein TTR are readily observed and distinguished from normal TTR. Free TTR as well as TTR-cysteine and TTR-cysteinylglycine adducts are clearly evident. The resulting assay from serum to final interpretation requires less than twenty minutes. The assay should be an effective first line discriminator of patients who are being considered to have Familial Amyloidotic Polyneuropathy (FAP) and an adjunct to definitive diagnosis by sequencing of the TTR gene or protein.
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