Marhaug G, Husby G
Clin Exp Immunol. 1981 Jul;45(1):97-106.
Human amyloid-related protein SAA has been prepared and purified by gel filtration, ion-exchange and affinity chromatography techniques. It was shown that SAA, even after extensive purification, is an electrophoretically heterogeneous protein. In addition, prealbumin and fragments of albumin were detected in the SAA preparation. Most of the SAA molecules and the fragments of albumin were present in a free form, but some SAA was also found to be complexed with albumin fragments.
人淀粉样相关蛋白SAA已通过凝胶过滤、离子交换和亲和层析技术制备并纯化。结果表明,即使经过广泛纯化,SAA仍是一种电泳不均一的蛋白质。此外,在SAA制剂中检测到了前白蛋白和白蛋白片段。大多数SAA分子和白蛋白片段以游离形式存在,但也发现一些SAA与白蛋白片段形成了复合物。