伴有红细胞增多症的IgM冷球蛋白血症表现为高黏滞综合征。II. 冷球蛋白形成的生化特性及机制

IgM pyroglobulinemia with erythrocytosis presenting as hyperviscosity syndrome. II. Biochemical properties and mechanisms of pyrogel formation.

作者信息

McCann S R, Zinneman H H, Oken M M, Sinha A A

出版信息

Am J Med. 1976 Sep;61(3):321-5. doi: 10.1016/0002-9343(76)90367-3.

Abstract

An immunoglobulin M with kappa light chains (IgMK) pyroglobulin from a patient with hyperviscosity syndrome, erythrocytosis and coagulation defects has been studied for its immunochemical properties. At physiologic temperatures the purified macropyroglobulin showed a striking tendency to aggregate in the pentamer as well as in the monomer form. This property was also observed in its H chains. Aggregate formation of the pentamers may have contributed to the blood viscosity and coagulation defects. Formation of pyrogel at 56degreesC was observed with pentamers as well as monomers, but not with separated H or L chains. Amino acid analysis showed quantitative abnormalities of aspartic acid, glycine, cystine and leucine within the H chains. Solubility of the pyrogel in sodium dodecyl sulfate, the pyroglobulin's tendency to aggregate and the cystine deficit of H chains implicate conformational changes leading to hydrophobic bonding at 56degreesC in the formation of pyrogel.

摘要

对一名患有高黏滞综合征、红细胞增多症和凝血缺陷患者的含κ轻链免疫球蛋白M（IgMK）热球蛋白的免疫化学特性进行了研究。在生理温度下，纯化的大分子量热球蛋白呈现出以五聚体和单体形式显著聚集的趋势。在其重链中也观察到了这种特性。五聚体的聚集体形成可能导致了血液黏度和凝血缺陷。在56℃时，五聚体和单体均观察到热凝胶的形成，但分离的重链或轻链则未出现。氨基酸分析显示重链内天冬氨酸、甘氨酸、胱氨酸和亮氨酸存在定量异常。热凝胶在十二烷基硫酸钠中的溶解性、热球蛋白的聚集趋势以及重链中的胱氨酸缺乏表明，在56℃时，构象变化导致疏水键合，从而形成热凝胶。