Skogen B, Thorsteinsson L, Natvig J B
Scand J Immunol. 1980;11(5):533-40. doi: 10.1111/j.1365-3083.1980.tb00021.x.
On incubation in cultures of blood mononuclear leucocytes from normal individuals, protein SAA is gradually degraded and yields an intermediate fragment with the same molecular weight as that of protein AA. This protein fragment has the same antigenic properties as protein AA, as judged from double-immunodiffusion analysis. Cell fractionation studies attribute the degrading capacity to the monocytes. Evidence was also found that the proteolytically active substances was released to the medium by cells in culture. The proteolytic substance, which also degraded protein AA, could be inhibited by diisopropyfluorophosphate and phenylmethyl sulfonylfluoride. This suggested that the enzyme might be a serine protease.
在来自正常个体的血液单核白细胞培养物中孵育时，蛋白质SAA会逐渐降解，并产生一个与蛋白质AA分子量相同的中间片段。根据双向免疫扩散分析判断，该蛋白质片段具有与蛋白质AA相同的抗原特性。细胞分级分离研究将降解能力归因于单核细胞。还发现有证据表明，蛋白水解活性物质由培养中的细胞释放到培养基中。这种也能降解蛋白质AA的蛋白水解物质可被二异丙基氟磷酸酯和苯甲基磺酰氟抑制。这表明该酶可能是一种丝氨酸蛋白酶。
