Is the Formation of AL-Type Amyloid Promoted by Structural Peculiarities of Immunoglobulin L-Chains? Primary Structure of an Amyloidogenic λ-L-Chain (BJP-ZIM)
- 1 January 1987
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 368 (2) , 863-870
- https://doi.org/10.1515/bchm3.1987.368.2.863
Abstract
A Bence-Jones protein (Protein ZIM) was isolated from the urine of a patient with myeloma-associated amyloidosis. The amino-acid sequence of the variable region of the carboxymethylated protein was established by automatic stepwise degradation of the enzymatically deblocked protein and tryptic peptides thereof. The protein is of the .lambda.-type of human immunoglobulin L-chains and is closely homologous to subgroup I. In the course of the tryptic digestion a precipitate was formed which showed properties characteristic of amyloid, such as staining with Congo red and green birefringence in polarized light. High-performance liquid chromatography was applied to separate these peptides. The precipitate consists of two peptides which coincide with position 19-45 of the variable and 129-140 of the constant part, respectively. Possible implications of this finding are discussed in the context of amyloid formation after limited proteolytic digestion.This publication has 11 references indexed in Scilit:
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