Characterization and quantification of mink serum amyloid A protein using two-dimensional electrophoresis with immobilized pH gradients.
Using hydrophobic interaction chromatography, two-dimensional electrophoresis with an immobilized pH gradient in the first dimension and semidry blotting, three isoforms of mink serum amyloid A protein (SAA) were characterized and studied during chronic inflammation. Compared to conventional methods that have been applied to SAA, the major advantages of the present combination of methods are: (i) use of small serum volumes, (ii) rapid extraction, (iii) high resolution, and (iv) high yield of proteins.
Bruun
C F
CF
Institute of Clinical Medicine, University of Tromsø, Norway.
Sletten
K
K
Husby
G
G
Marhaug
G
G
D000210:Acute-Phase Reaction / Q000097:blood; D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D007249:Inflammation / Q000097:blood / Q000139:chemically induced; D007526:Isoelectric Point; D008070:Lipopolysaccharides; D008907:Mink / Q000097:blood*; D000685:Serum Amyloid A Protein / Q000032:analysis*
D008070:Lipopolysaccharides; D000685:Serum Amyloid A Protein