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The amino-acid sequence of the variable region of a carbohydrate-containing amyloid fibril protein EPS of immunoglobulin lambda light chain origin has been elucidated. The protein was isolated from the liver of a patient (EPS) with an immunocyte dyscrasia of the IgM type. The molecular mass of this protein was found to be about 20 kDa including an oligosaccharide chain linked to it. The amino-acid sequence determination involved automatic Edman degradation of polypeptides obtained after cleaving the protein with BNPS-skatole, trypsin and thermolysin. The proposed sequence of the variable region of the protein showed that it may be assigned to the V lambda I subgroup. A tryptic and a thermolysinolytic peptide both containing the carbohydrate were isolated and characterized, and the localization of an oligosaccharide chain linked to asparagine was established.
K G Toft, and
K Sletten, and
G Husby
November 1985,
The Biochemical journal,
K G Toft, and
K Sletten, and
G Husby
June 1981,
The Biochemical journal,
K G Toft, and
K Sletten, and
G Husby
November 1986,
The Biochemical journal,
K G Toft, and
K Sletten, and
G Husby
September 1990,
The Journal of investigative dermatology,
K G Toft, and
K Sletten, and
G Husby
November 1975,
Proceedings of the National Academy of Sciences of the United States of America,
K G Toft, and
K Sletten, and
G Husby
January 1974,
Scandinavian journal of immunology,
K G Toft, and
K Sletten, and
G Husby
May 1997,
Scandinavian journal of immunology,
K G Toft, and
K Sletten, and
G Husby
August 1993,
Biochemical and biophysical research communications,
K G Toft, and
K Sletten, and
G Husby
May 1978,
Biochemistry,
K G Toft, and
K Sletten, and
G Husby
December 1970,
Biochemical and biophysical research communications,
