一名原发性淀粉样变性患者的糖基化AL链的氨基酸序列。

The amino acid sequence of a glycosylated AL-chain from a patient with primary amyloidosis.

作者信息

Myran Theresa, Husby Gunnar, Kyle Robert A, Sletten Knut

机构信息

Biotechnology Centre of Oslo, University of Oslo, Norway.

出版信息

Amyloid. 2004 Jun;11(2):109-12. doi: 10.1080/13506120412331272278.

DOI:10.1080/13506120412331272278

PMID:15478466

Abstract

An amyloid fibril protein (Owe) related to primary amyloidosis was found to be a glycosylated complete immunoglobulin light chain (AL). The amino acid sequence revealed a protein composed of 214 residues and with a glycosylation site in position 20. The sequence established an AL V-region corresponding to a kappa 1b germline gene, but differs from that in 12 positions. Eight of them are in the FR-regions, positions 7, 13, 20, 42, 46, 60, 76 and 79. The J-segment is that of JkappaII.

摘要

一种与原发性淀粉样变性相关的淀粉样纤维蛋白（Owe）被发现是一种糖基化的完整免疫球蛋白轻链（AL）。氨基酸序列显示该蛋白由214个残基组成，在第20位有一个糖基化位点。该序列确定了一个与κ1b种系基因相对应的AL V区，但在12个位置上与之不同。其中8个位于FR区，即第7、13、20、42、46、60、76和79位。J片段是JκII的片段。