Partial purification and characterization of hemolysin from the coelomic fluid of Strongylocentrotus nudus

1. 1. This study was undertaken to partially purify the hemolysin from the coelomic fluid of Strongylocentrotus nudus by a combination of affinity, hydrophobic and gel filtration chromatographies, and to investigate the property of this molecule. 2. 2. The hemolysin was purified about 120-fold by gel filtration and the chromatographic behavior indicated that the intact molecule of the hemolysin had a molecular mass of 200 kDa. 3. 3. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, under non-reducing condition, a single band of 40 kDa protein disappeared with absorption by rabbit and sheep erythrocytes. 4. 4. It was suggested that this hemolysin molecule, with a single subunit of 40 kDa, had a physiological function as an opsonin.