Isolation of serum amyloid A protein by small-scale hydrophobic interaction chromatography and two-dimensional electrophoresis.
A recently introduced technique to isolate serum amyloid A protein is hydrophobic interaction chromatography combined with two-dimensional electrophoresis with immobilized pH gradients. A modification of the original version of this technique is presented. Mouse serum was subjected to hydrophobic interaction chromatography on a small scale, and the eluate was applied directly to two-dimensional electrophoresis. Simple electropherogramss with optimal resolution of serum amyloid A protein were obtained. The presented technique facilitates isolation of serum amyloid A protein from small blood volumes, and might also be adapted to alternative applications.
Bruun
C F
CF
Paediatric Research Laboratorium, University of Tromsø, Norway.
Sletten
K
K
Mehlum
A
A
Marhaug
G
G
D000818:Animals; D002847:Chromatography, Agarose / Q000379:methods*; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D007274:Injections, Intraperitoneal; D051379:Mice; D008810:Mice, Inbred C57BL; D000685:Serum Amyloid A Protein / Q000008:administration & dosage / Q000737:chemistry / Q000302:isolation & purification*; D016622:Silver Staining; D013499:Surface Properties
D000685:Serum Amyloid A Protein