The Amino-Acid Sequence of the Variable Region of a Carbohydrate-Containing Amyloid Fibril Protein EPS (Immunoglobulin Light Chain, Type λ)
- 1 January 1985
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 366 (2) , 617-626
- https://doi.org/10.1515/bchm3.1985.366.2.617
Abstract
The amino-acid sequence of the variable region of a carbohydrate-containing amyloid fibril protein EPS of Ig .lambda. light chain origin was 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 [Kdalton] 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.This publication has 12 references indexed in Scilit:
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