Ohno T, Furukawa H, Kanoh T, Uchino H
Clin Chim Acta. 1986 Nov 15;160(3):235-43. doi: 10.1016/0009-8981(86)90190-7.
The extremely rare IgD pyroglobulin caused opalescence, lost its antigenicity and acquired more negative charge when heated for 30 min at 56 degrees C. Exposure to 60 degrees C for 60 min produced a firm gel. The thermoprecipitability was abolished by the treatment with guanidine, urea and sodium dodecyl sulfate, but not by 2-mercaptoethanol or neuraminidase, and required the presence of both heavy and light chains. However, amino acid analysis showed abnormalities only in the heavy chain. We hypothesize that the irreversible heat-induced aggregation of IgD pyroglobulin is the result of a conformational change, triggered by light chain, which increases the molecular hydrophobicity.
极为罕见的IgD热球蛋白在56℃加热30分钟时会出现乳光现象,失去抗原性并获得更多负电荷。在60℃暴露60分钟会形成坚固的凝胶。用胍、尿素和十二烷基硫酸钠处理可消除热沉淀性,但2-巯基乙醇或神经氨酸酶处理则不能,且热沉淀需要重链和轻链同时存在。然而,氨基酸分析显示只有重链存在异常。我们推测,IgD热球蛋白不可逆的热诱导聚集是由轻链引发的构象变化导致的,这种变化增加了分子的疏水性。