Primary structure of the variable region of an amyloidogenic Bence Jones protein NIG-77
Autor: | Takashi Isobe, Fuyuki Kametani, Akihiko Hoshi, Hiroshi Tonoike, Tomotaka Shinoda |
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Rok vydání: | 1985 |
Předmět: |
Chemical Phenomena
Stereochemistry Biophysics Immunoglobulin light chain Biochemistry Homology (biology) Humans Trypsin Amino Acid Sequence Amino Acids Molecular Biology Peptide sequence Chromatography High Pressure Liquid Chemistry Protein primary structure Amyloidosis Cell Biology Middle Aged Systemic amyloidosis Peptide Fragments Bence Jones protein Proteinuria Female Multiple Myeloma Bence Jones Protein |
Zdroj: | Biochemical and Biophysical Research Communications. 126:1228-1234 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(85)90317-1 |
Popis: | 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. |
Databáze: | OpenAIRE |
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