Gunnarsson M, Stigbrand T, Jensen P E
Department of Immunology, Umeå University, Sweden.
Acta Neurol Scand. 2000 Apr;101(4):270-2. doi: 10.1034/j.1600-0404.2000.101004270.x.
To investigate conformational properties of alpha2-macroglobulin from multiple sclerosis patients.
alpha2-macroglobulin was purified to homogeneity from plasma of 4 multiple sclerosis patients and 5 healthy controls. The plasma and the purified alpha2-macroglobulin from each individual were investigated using polyacrylamide gel electrophoresis.
Impaired stability of purified alpha2-macroglobulins from multiple sclerosis patients was demonstrated with spontaneous conversion to an electrophoretic "fast" form upon purification and following storage not ascribable to bait region cleavage.
alpha2-macroglobulin from multiple sclerosis patients displays altered stability. Possible functional impairments of proteinase inhibition mechanisms are discussed.
研究多发性硬化症患者α2-巨球蛋白的构象特性。
从4例多发性硬化症患者和5例健康对照者的血浆中纯化α2-巨球蛋白至均一性。使用聚丙烯酰胺凝胶电泳对每个个体的血浆和纯化的α2-巨球蛋白进行研究。
多发性硬化症患者纯化的α2-巨球蛋白稳定性受损，纯化后以及储存后会自发转化为电泳“快”型，这并非由于诱饵区裂解所致。
多发性硬化症患者的α2-巨球蛋白显示出稳定性改变。讨论了蛋白酶抑制机制可能存在的功能损害。
