Eulitz M, Linke R P
GSF Institut f.Klinische Molekularbiologie, München, Germany.
Biochem Biophys Res Commun. 1993 Aug 16;194(3):1427-34. doi: 10.1006/bbrc.1993.1984.
The putative precursor molecule of a human AL type amyloid fibril protein was isolated from an ultrafiltrate after hemofiltration. Subsequent 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 lambda-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.
从血液滤过后的超滤液中分离出了人AL型淀粉样原纤维蛋白的假定前体分子。在二硫键还原和羧甲基化后，通过高效液相色谱（HPLC）对该蛋白质进行了后续分离。该蛋白质被分离成几个组分，通过自动氨基酸序列测定对其进行了进一步分析。从序列数据推断，前体分子是λ型免疫球蛋白L链。该蛋白质的V区与II亚组的蛋白质关系最为密切。在第110、129和179位的赖氨酸残基之后，分子内部发生了裂解。主要片段从第9位的丝氨酸或丙氨酸开始，延伸至V区第65位的丝氨酸。从这些片段产生的胰蛋白酶肽几乎覆盖了L链的整个V区和C区，但第1 - 8位除外，从该区域未分离出肽段。
