Bruun C F, Sletten K, Husby G, Marhaug G
Institute of Clinical Medicine, University of Tromsø, Norway.
Electrophoresis. 1993 Dec;14(12):1372-4. doi: 10.1002/elps.11501401211.
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.
利用疏水相互作用色谱法、第一维采用固定化pH梯度的二维电泳法以及半干印迹法，对水貂血清淀粉样蛋白A（SAA）的三种同工型在慢性炎症过程中进行了表征和研究。与应用于SAA的传统方法相比，本方法组合的主要优点是：（i）使用少量血清，（ii）快速提取，（iii）高分辨率，以及（iv）蛋白质高产率。
