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Macromolecular Properties of Glycosaminoglycans in Primary AL Amyloid Fibril Extracts of Lymphoid Tissue Origin
Author(s) -
STENSTAD T.,
MAGNUS J. H.,
KOLSET S. O.,
CORNWELL G. G.,
HUSBY G.
Publication year - 1991
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1991.tb01584.x
Subject(s) - glycosaminoglycan , chemistry , dermatan sulfate , amyloidosis , size exclusion chromatography , fibril , amyloid (mycology) , amyloid fibril , biochemistry , spleen , heparan sulfate , amyloid β , pathology , immunology , biology , medicine , enzyme , inorganic chemistry , disease
We have previously demonstrated the presence of glycosaminoglycans (GAGs) in water extracts of secondary A A amyloid fibrils. In the present study we isolated significant quantities of GAGs from fibril extracts of immunoglobulin light chain (AL) type derived from the spleens from two patients afflicted with primary amyloidosis. Employing ion‐exchange chromatography and gel filtration subsequent lo various specific chemical and enzymalic treatments, different types of high molecular weight GAGs were found in both preparations, but not in the corresponding normal splenic extracts. The amyloid‐associated GAGs of the extracts derived from one patient consisted of 60% dermatan sulphate and 40% n heparan sulphate whereas those obtained from the second spleen were 25% dermatan sulphate and 75% heparan sulphate. The heparan sulphate fraction occurred in the form of proteoglycans, whereas the dermatan sulphate apparently occurred as free GAG chains, resembling the data recently obtained from AA amyloid fibril extracts.