Eulitz M, Breuer M, Linke R P
Biol Chem Hoppe Seyler. 1987 Jul;368(7):863-70. doi: 10.1515/bchm3.1987.368.2.863.
A Bence-Jones protein (Protein ZIM) was isolated from the urine of a patient with myeloma-associated amyloidosis. The amino-acid sequence of the variable region of the carboxymethylated protein was established by automatic stepwise degradation of the enzymatically deblocked protein and tryptic peptides thereof. The protein is of the lambda-type of human immunoglobulin L-chains and is closely homologous to subgroup I. In the course of the tryptic digestion a precipitate was formed which showed properties characteristic of amyloid, such as staining with Congo red and green birefringence in polarized light. High-performance liquid chromatography was applied to separate these peptides. The precipitate consists of two peptides which coincide with position 19-45 of the variable and 129-140 of the constant part, respectively. Possible implications of this finding are discussed in the context of amyloid formation after limited proteolytic digestion.
从一名患有骨髓瘤相关性淀粉样变性患者的尿液中分离出一种本-周蛋白（蛋白ZIM）。通过对酶解去封闭蛋白及其胰蛋白酶肽段进行自动逐步降解，确定了羧甲基化蛋白可变区的氨基酸序列。该蛋白属于人免疫球蛋白L链的λ型，与I亚组密切同源。在胰蛋白酶消化过程中形成了一种沉淀物，其表现出淀粉样蛋白的特征特性，如刚果红染色和偏振光下的绿色双折射。应用高效液相色谱法分离这些肽段。沉淀物由两种肽段组成，分别与可变区的第19 - 45位和恒定区的第129 - 140位一致。在有限蛋白水解消化后淀粉样蛋白形成的背景下讨论了这一发现的可能意义。
