title: Decreased stability of alpha2-macroglobulin purified from patients with multiple sclerosis.
abstract: 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.
authors.affiliation: Department of Immunology, Umeå University, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Gunnarsson
authors.forename: T
authors.initials: T
authors.lastname: Stigbrand
authors.forename: P E
authors.initials: PE
authors.lastname: Jensen
mesh_terms: 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
chemical_list: D011480:Protease Inhibitors; D000511:alpha-Macroglobulins