Johansson S G, Bennich H
Immunology. 1967 Oct;13(4):381-94.
An 8S myeloma component, isolated from serum of a patient with myelomatosis is described, which appears to have no antigenic determinants in common with human, α-, δ-, γ- or μ-polypeptide chains as revealed by immuno-electrophoresis and Ouchterlony gel diffusion analysis. The myeloma protein migrates in the fast γ-region on electrophoresis at pH 8.6 and has an elution volume on Sephadex G-200 similar to that of 6.5S IgA. The isolated myeloma component has an approximate molecular weight of 200,000 and a total carbohydrate content of 10.7 per cent. Reduction with β-mercaptoethanol and acid dissociation yields light polypeptide chains of Type L and a carbohydrate-rich component, in the ratio of 1:4. Antisera specific to determinants on the heavy chains of the myeloma protein showed no reaction with the immunoglobulins A, D, G or M. Instead unique determinants were found on the heavy polypeptide chains.
本文描述了从一例骨髓瘤病患者血清中分离出的一种8S骨髓瘤成分，免疫电泳和双向免疫扩散分析显示，该成分似乎与人α-、δ-、γ-或μ-多肽链没有共同的抗原决定簇。骨髓瘤蛋白在pH 8.6电泳时在快速γ区迁移，在Sephadex G - 200上的洗脱体积与6.5S IgA相似。分离出的骨髓瘤成分的分子量约为200,000，总碳水化合物含量为10.7%。用β-巯基乙醇还原和酸解离产生L型轻多肽链和富含碳水化合物的成分，比例为1:4。针对骨髓瘤蛋白重链上决定簇的特异性抗血清与免疫球蛋白A、D、G或M无反应。相反，在重多肽链上发现了独特的决定簇。
