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Discussion In the present report the structure of two new κ 1 -LCDD proteins, GLA and CHO, obtained by N-terminal sequence analysis of light chain deposits extracted from the tissues, light chains isolated from the urines, and the V-region amino acid side deduced from the cloned and sequenced cDNAs, and MCM, 11 are compared to the germline sequence determined from genomic DNA in. No staining for λ light chain. In AL, although the primary protein structure likely plays an important role in fibril formation, amyloidogenic motifs have not been identified in the primary sequence data of more than 60 light chains extracted from amyloid tissue deposits. Sections were incubated with a panel of fluorescein-labeled rabbit polyclonal anti-human Ig chain-specific antibodies γ, μ, α, κ, and λC3, C1q, fibrin and unlabeled rabbit polyclonals anti-amyloid P Jeg gir en kobling Dako, Carpenteria, CAand anti-apo-E Chemicon, Temecula, CAfollowed by fluorescein-conjugated swine anti-rabbit Ig Dako. The reason s for their differences are unknown but are likely multifactorial and related to their protein conformation and their interaction with other molecules and tissue factors in the microenvironment.

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