来自单体尾索动物柄海鞘的一种体液调理素的纯化与特性分析。

Purification and characterization of a humoral opsonin from the solitary urochordate Styela clava.

Kelly K L, Cooper E L, Raftos D A

Department of Anatomy and Cell Biology, School of Medicine, University of California, Los Angeles 90024.

Comp Biochem Physiol B. 1992 Nov;103(3):749-53. doi: 10.1016/0305-0491(92)90401-c.

Abstract

We have previously identified opsonic activity in the plasma of the solitary urochordate, Styela clava. 2. Here, we report the purification and further characterization of the opsonic molecule. 3. Two purification methods were employed. 4. Gel filtration yielded one strongly opsonic fraction that contained a single, electrophoretically-resolved protein. 5. Opsonic activity was dose-dependent and sensitive to tryptic digestion and heat denaturation. 6. SDS-PAGE and calibrated gel filtration indicated the opsonic protein was a 17.5 kDa monomer while isoelectrofocusing indicated a single pI of 7.0. 7. In an alternative procedure, a similar opsonic activity and protein were isolated by affinity purification using whole yeast cells.

摘要

我们之前已在单体尾索动物柄海鞘的血浆中鉴定出调理活性。2. 在此，我们报告调理分子的纯化及进一步特性分析。3. 采用了两种纯化方法。4. 凝胶过滤产生了一个强调理活性组分，其中包含一种经电泳分离的单一蛋白质。5. 调理活性呈剂量依赖性，对胰蛋白酶消化和热变性敏感。6. SDS - 聚丙烯酰胺凝胶电泳和校准凝胶过滤表明，调理蛋白是一种17.5 kDa的单体，而等电聚焦显示单一pI为7.0。7. 在另一种方法中，使用全酵母细胞通过亲和纯化分离出了类似的调理活性和蛋白质。