1. 1. We have previously identified opsonic activity in the plasma of the solitary urochordate, Styela clava. 2. 2. Here, we report the purification and further characterization of the opsonic molecule. 3. 3. Two purification methods were employed. 4. 4. Gel filtration yielded one strongly opsonic fraction that contained a single, electrophoretically-resolved protein. 5. 5. Opsonic activity was dose-dependent and sensitive to tryptic digestion and heat denaturation. 6. 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. 7. In an alternative procedure, a similar opsonic activity and protein were isolated by affinity purification using whole yeast cells.
|Number of pages||5|
|Journal||Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology|
|Publication status||Published - 1992|