摘要
用低亲和力组织型纤溶酶原激活剂(tpA)A链单克在抗体制备了免疫亲和层析柱,纯化50OmlBowes细胞无血清培液中的tpA,回收率达75%,经SDS一PAGE电泳证实纯化的洗脱液蛋白的分子量为67kd,仅呈一条带,用发色底物法(S2390)测定表明洗脱液蛋白具有tpA活性。
mmunoaffinity chromatographic column Was prepared with low affinity monoclonal anti-body against A chain of tissue一type plasminogen activator. tpA was purified from 500ml BOwescell culture without serum. The rate of recovery was up to 75%. Through SDS一PAGE elec- trophoresis it was proven that the molecular weight of the eluted protein purifed was 67 Kd andonly one band was presented. The tpA activity of the eluted protein was identified with chro- mogenic substrate(S2390).
出处
《温州医学院学报》
CAS
1995年第1期7-9,共3页
Journal of Wenzhou Medical College