Abstract:
:In AL-amyloidosis the cause of amyloid fibril formation in beta-pleated sheets from the precursor protein immunoglobulin light chain is not established, but studies of AL-proteins indicate that amino acid substitutions are important in the pathogenesis. Amyloid material was extracted from a subcutaneous fat tissue biopsy and submitted to extended protein separation, typing and amino acid sequence analyses. The AL-protein belonged to the rare immunoglobulin light chain kappa, subtype kappa IV and contained unique amino acid substitutions, mostly in the highly preserved framework regions. The study shows that subcutaneous fat biopsies are useful sources of amyloid material for biochemical studies.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Olsen KE,Sletten K,Westermark Pdoi
10.1006/bbrc.1998.8515subject
Has Abstractpub_date
1998-04-28 00:00:00pages
713-6issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(98)98515-1journal_volume
245pub_type
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