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. 1985 Feb 15;126(3):1228-34.
doi: 10.1016/0006-291x(85)90317-1.

Primary structure of the variable region of an amyloidogenic Bence Jones protein NIG-77

Primary structure of the variable region of an amyloidogenic Bence Jones protein NIG-77

H Tonoike et al. Biochem Biophys Res Commun. .

Abstract

The complete amino acid sequence of the variable region of a Bence Jones protein NIG-77 from an individual with myeloma-associated systemic amyloidosis has been determined. This protein represents a complete light chain consisting of 216 residues and it has a sequence characteristic of V lambda I subgroup, which is closely homologous to that of another amyloidogenic V lambda I Bence Jones protein NIG-51, differing by 20 of 111 residues (82% homology). In contrast, it differs by 29 residues (74% homology) to that of non-amyloidogenic V lambda I light chain NIG-64. This finding shows that, in accordance with our previous report(1), the V lambda I-related light chains can further be divided into two distinct subsubgroups, V lambda I-1 and V lambda I-2, and the latter property seems to be more prone in association with the amyloid process.

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