PuSH - Publikationsserver des Helmholtz Zentrums München: The precursor molecule of A Vλ II-immunoglobulin light chain-derived amyloid fibril protein circulates precleaved.

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Eulitz, M. ; Linke, R.P.

The precursor molecule of A Vλ II-immunoglobulin light chain-derived amyloid fibril protein circulates precleaved.

Biochem. Biophys. Res. Commun. 194, 1427-1434 (1993)

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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.

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The putative precursor molecule of a human AL type amyloid fibril protein was isolated from an ultrafiltrate after hemofiltration. Subsequennt separation of this protein was achieved by high performance liquid chromatography (HPLC) after reduction and carboxymethylation of the disulfide bonds. The protein was separated into several fractions which were further analyzed by automatic amino acid sequence determination. It was deduced from the sequence data that the precursor molecule is an immunoglobulin L-chain of the λ-type. The V-region of this protein is most closely related to the proteins of subgroup II. Internal splits occurred in the molecule after lysine residues in positions 110, 129 and 179. The predominant fragment commences with either serine or alanine in position 9 and extends to a serine in position 65 of the V-region. Tryptic peptides generated from the fragments cover nearly the entire V- and C-region of the L-chain, with the exception of positions 1-8, from which no peptide has been isolated.

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