Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin.

作者：Mordechai Pras, Frances Prelli, E. C. Franklin, Bias Frangione · 发表于：Proceedings of the National Academy of Sciences · 年份：1983 · DOI：10.1073/pnas.80.2.539 · 被引用次数：115 · 研究领域：Amyloidosis: Diagnosis, Treatment, Outcomes、Dermatological and Skeletal Disorders、Alkaline Phosphatase Research Studies

The complete amino acid sequence of three related amyloid proteins (Mr 14,000, 10,000, and 5,000) derived from tissues of a Jewish patient who suffered from a variant of familial polyneuropathic amyloidosis was determined. The protein, which contains 127 residues, is identical to a human serum prealbumin subunit. Only one amino acid substitution, glycine for threonine, was detected at position 49, where enzymatic cleavage occurred, yielding Mr 5,000 and 10,000 fragments which represent the amino terminus (residues 1-48) and carboxyl terminus (residues 49-127) of the molecule, respectively. Thus, a prealbumin variant and its fragments constitute the amyloid fibrils in a heredofamilial amyloidosis syndrome of dominant inheritance.