Decreased stability of alpha(2)-macroglobulin purified from patients with multiple sclerosis

(C) Munksgaard 2000. Objectives - To investigate conformational properties of alpha(2)-macroglobulin from multiple sclerosis patients. Materials and m ethods alpha(2)-macroglobulin was purified to homogeneity from plasma of 4 multiple sclerosis patients and 5 healthy controls. The plasma and the puri fied alpha(2)-macroglobulin from each individual were investigated using po lyacrylamide gel electrophoresis. Results - Impaired stability of purified alpha(2)-macroglobulins from multiple sclerosis patients was demonstrated w ith spontaneous conversion to an electrophoretic "fast" form upon purificat ion and following storage not ascribable to bait region cleavage. Conclusio n - alpha(2)-macroglobulin from multiple sclerosis patients displays altere d stability. Possible functional impairments of proteinase inhibition mecha nisms are discussed.