Decreased stability of alpha2-macroglobulin purified from patients with multiple sclerosis.
OBJECTIVE
To investigate conformational properties of alpha2-macroglobulin from multiple sclerosis patients.


METHODS
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.


RESULTS
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.


CONCLUSIONS
alpha2-macroglobulin from multiple sclerosis patients displays altered stability. Possible functional impairments of proteinase inhibition mechanisms are discussed.
Gunnarsson
M
M
Department of Immunology, Umeå University, Sweden.
Stigbrand
T
T
Jensen
P E
PE
D000328:Adult; D016022:Case-Control Studies; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D008297:Male; D009103:Multiple Sclerosis / Q000097:blood*; D011480:Protease Inhibitors / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D000511:alpha-Macroglobulins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
D011480:Protease Inhibitors; D000511:alpha-Macroglobulins