HUMAN-SERUM AMYLOID-A PROTEIN - BEHAVIOR IN AQUEOUS AND UREA-CONTAINING SOLUTIONS AND ANTIBODY-PRODUCTION
HUMAN-SERUM AMYLOID-A PROTEIN - BEHAVIOR IN AQUEOUS AND UREA-CONTAINING SOLUTIONS AND ANTIBODY-PRODUCTION
复制标题
DOI：
10.1042/bj2630365
复制
发表时间：
1989-10-15
影响因子：
4.1
通讯作者：
DEBEER, FC
中科院分区：
文献类型：
--
作者：
STRACHAN, AF;SHEPHARD, EG;DEBEER, FC
Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (> 90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at > 7 M-urea. By immunizing with apo-SAA adsorbed to acid-treated bacteria (Salmonella minnesota R595), high-titre antibodies can esily be elicited in rabbits.
