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Characterization and quantification of mink serum amyloid A protein using two‐dimensional electrophoresis with immobilized pH gradients
Author(s) -
Bruun Cathrine Foyn,
Sletten Knut,
Husby Gunnar,
Marhaug Gudmund
Publication year - 1993
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.11501401211
Subject(s) - mink , chromatography , chemistry , electrophoresis , blot , serum amyloid a , amyloid (mycology) , high resolution , protein purification , resolution (logic) , biochemistry , inflammation , biology , immunology , inorganic chemistry , ecology , remote sensing , gene , geology , artificial intelligence , computer science
Abstract 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.